IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Comprehensive identification of Arabidopsis thaliana MYB transcription factors interacting with R/B-like BHLH proteins. Comprehensive identification of Arabidopsis thaliana MYB transcription factors interacting with R/B-like BHLH proteins. Plant J. (0960-7412) 2004 Zimmermann IM., Heim MA., Weisshaar B., Uhrig JF. bernd.weisshaar@uni-bielefeld.de 22-Jan-2008: Contacted by JYOTI. orchard yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Zimmermann IM., Heim MA., Weisshaar B., Uhrig JF. bernd.weisshaar@uni-bielefeld.de Accepted 2007-DEC-6 by ORCHARD. 22-Jan-2008: Contacted by JYOTI. Arabidopsis whole plant and cell culture cDNA libraries Plant J. (0960-7412) 2004 orchard Comprehensive identification of Arabidopsis thaliana MYB transcription factors interacting with R/B-like BHLH proteins. Comprehensive identification of Arabidopsis thaliana MYB transcription factors interacting with R/B-like BHLH proteins. Plant J. (0960-7412) 2004 Zimmermann IM., Heim MA., Weisshaar B., Uhrig JF. bernd.weisshaar@uni-bielefeld.de 22-Jan-2008: Contacted by JYOTI. orchard yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Zimmermann IM., Heim MA., Weisshaar B., Uhrig JF. bernd.weisshaar@uni-bielefeld.de Accepted 2007-DEC-6 by ORCHARD. Plant J. (0960-7412) 2004 orchard Comprehensive identification of Arabidopsis thaliana MYB transcription factors interacting with R/B-like BHLH proteins. Comprehensive identification of Arabidopsis thaliana MYB transcription factors interacting with R/B-like BHLH proteins. Plant J. (0960-7412) 2004 Zimmermann IM., Heim MA., Weisshaar B., Uhrig JF. bernd.weisshaar@uni-bielefeld.de 22-Jan-2008: Contacted by JYOTI. orchard in vitro In vitro pull down pull down predetermined predetermined participant predetermined Zimmermann IM., Heim MA., Weisshaar B., Uhrig JF. bernd.weisshaar@uni-bielefeld.de Accepted 2007-DEC-6 by ORCHARD. 22-Jan-2008: Contacted by JYOTI. Plant J. (0960-7412) 2004 orchard my113_arath Transcription factor MYB113 MYB113 At1g66370 Myb-related protein 113 T27F4.12 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGESPKGLRKGTWTTEEDILLRQCIDKYGEGKWHRVPLRTGLNRCRKSCRLRWLNYLKPSIKRGKLCSDEVDLVLRLHKLLGNRWSLIAGRLPGRTANDVKNYWNTHLSKKHDERCCKTKMINKNITSHPTSSAQKIDVLKPRPRSFSDKNSCNDVNILPKVDVVPLHLGLNNNYVCESSITCNKDEQKDKLININLLDGDNMWWESLLEADVLGPEATETAKGVTLPLDFEQIWARFDEETLELN FF1C4B9176040D20 myb23_arath Transcription factor MYB23 MYB23 MPO12.5 At5g40330 Myb-related protein 23 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MRMTRDGKEHEYKKGLWTVEEDKILMDYVRTHGQGHWNRIAKKTGLKRCGKSCRLRWMNYLSPNVNRGNFTDQEEDLIIRLHKLLGNRWSLIAKRVPGRTDNQVKNYWNTHLSKKLGLGDHSTAVKAACGVESPPSMALITTTSSSHQEISGGKNSTLRFDTLVDESKLKPKSKLVHATPTDVEVAATVPNLFDTFWVLEDDFELSSLTMMDFTNGYCL 774DE100200B50FF myb5_arath Transcription repressor MYB5 MYB5 At3g13540 M2 Myb-related protein 5 AtM2 MRP15.2 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MMSCGGKKPVSKKTTPCCTKMGMKRGPWTVEEDEILVSFIKKEGEGRWRSLPKRAGLLRCGKSCRLRWMNYLRPSVKRGGITSDEEDLILRLHRLLGNRWSLIAGRIPGRTDNEIKNYWNTHLRKKLLRQGIDPQTHKPLDANNIHKPEEEVSGGQKYPLEPISSSHTDDTTVNGGDGDSKNSINVFGGEHGYEDFGFCYDDKFSSFLNSLINDVGDPFGNIIPISQPLQMDDCKDGIVGASSSSLGHD AFDEFA57222B2424 bh012_arath Transcription factor MYC1 At4g00480 BHLH12 EN58 MYC1 Transcription factor EN 58 bHLH transcription factor bHLH012 Basic helix-loop-helix protein 12 F6N23.22 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MSLTMADGVEAAAGRSKRQNSLLRKQLALAVRSVQWSYAIFWSSSLTQPGVLEWGEGCYNGDMKKRKKSYESHYKYGLQKSKELRKLYLSMLEGDSGTTVSTTHDNLNDDDDNCHSTSMMLSPDDLSDEEWYYLVSMSYVFSPSQCLPGRASATGETIWLCNAQYAENKLFSRSLLARSASIQTVVCFPYLGGVIELGVTELISEDHNLLRNIKSCLMEISAHQDNDDEKKMEIKISEEKHQLPLGISDEDLHYKRTISTVLNYSADRSGKNDKNIRHRQPNIVTSEPGSSFLRWKQCEQQVSGFVQKKKSQNVLRKILHDVPLMHTKRMFPSQNSGLNQDDPSDRRKENEKFSVLRTMVPTVNEVDKESILNNTIKYLQELEARVEELESCMGSVNFVERQRKTTENLNDSVLIEETSGNYDDSTKIDDNSGETEQVTVFRDKTHLRVKLKETEVVIEVRCSYRDYIVADIMETLSNLHMDAFSVRSHTLNKFLTLNLKAKFRGAAVASVGMIKRELRRVIGDLF DIP protein Q8W2F1 original sequence version: 89 1E090B0EB5A107F3 q9c9a5_arath ARABIDOPSIS MYB-LIKE 2 ATMYBL2 MYB-like 2 MYBL2 F23N20.2 F23N20_2 At1g71030 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MNKTRLRALSPPSGMQHRKRCRLRGRNYVRPEVKQRNFSKDEDDLILKLHALLGNRWSLIAGRLPGRTDNEVRIHWETYLKRKLVKMGIDPTNHRLHHHTNYISRRHLHSSHKEHETKIISDQSSSVSESCGVTILPIPSTNCSEDSTSTGRSHLPDLNIGLIPAVTSLPALCLQDSSESSTNGSTGQETLLLFR DIP protein Q9C9A5 original sequence version: 94 B270E3414A015967 etc2_arath MYB-like transcription factor ETC2 ETC2 Protein ENHANCER OF TRY AND CPC 2 T6B20 T9D9 At2g30420 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MDNTNRLRLRRGPSLRQTKFTRSRYDSEEVSSIEWEFISMTEQEEDLISRMYRLVGNRWDLIAGRVVGRKANEIERYWIMRNSDYFSHKRRRLNNSPFFSTSPLNLQENLKL C7C86DDF9E5A4873 etc1_arath MYB-like transcription factor ETC1 ETC1 Protein ENHANCER OF TRY AND CPC 1 F6F3.18 At1g01380 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MNTQRKSKHLKTNPTIVASSSEEVSSLEWEEIAMAQEEEDLICRMYKLVGERWDLIAGRIPGRTAEEIERFWVMKNHRRSQLR 3D4802F360042860 egl1_arath Transcription factor EGL1 Protein ENHANCER OF GLABRA 3 Basic helix-loop-helix protein 2 BHLH2 EGL3 EGL1 MYC146 At1g63650 F24D7.16 EN30 Transcription factor EN 30 bHLH transcription factor bHLH002 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MATGENRTVPDNLKKQLAVSVRNIQWSYGIFWSVSASQPGVLEWGDGYYNGDIKTRKTIQAAEVKIDQLGLERSEQLRELYESLSLAESSASGSSQVTRRASAAALSPEDLTDTEWYYLVCMSFVFNIGEGIPGGALSNGEPIWLCNAETADSKVFTRSLLAKSASLQTVVCFPFLGGVLEIGTTEHIKEDMNVIQSVKTLFLEAPPYTTISTRSDYQEIFDPLSDDKYTPVFITEAFPTTSTSGFEQEPEDHDSFINDGGASQVQSWQFVGEEISNCIHQSLNSSDCVSQTFVGTTGRLACDPRKSRIQRLGQIQEQSNHVNMDDDVHYQGVISTIFKTTHQLILGPQFQNFDKRSSFTRWKRSSSVKTLGEKSQKMIKKILFEVPLMNKKEELLPDTPEETGNHALSEKKRREKLNERFMTLRSIIPSISKIDKVSILDDTIEYLQDLQKRVQELESCRESADTETRITMMKRKKPDDEEERASANCMNSKRKGSDVNVGEDEPADIGYAGLTDNLRISSLGNEVVIELRCAWREGILLEIMDVISDLNLDSHSVQSSTGDGLLCLTVNCKHKGTKIATTGMIQEALQRVAWIC 6B934DFBE82AA102 myb75_arath Transcription factor MYB75 MYB75 PAP1 SIAA1 F25P12.92 At1g56650 Myb-related protein 75 Production of anthocyanin pigment 1 protein Suc-induced anthocyanin accumulation locus 1 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MEGSSKGLRKGAWTTEEDSLLRQCINKYGEGKWHQVPVRAGLNRCRKSCRLRWLNYLKPSIKRGKLSSDEVDLLLRLHRLLGNRWSLIAGRLPGRTANDVKNYWNTHLSKKHEPCCKIKMKKRDITPIPTTPALKNNVYKPRPRSFTVNNDCNHLNAPPKVDVNPPCLGLNINNVCDNSIIYNKDKKKDQLVNNLIDGDNMWLEKFLEESQEVDILVPEATTTEKGDTLAFDVDQLWSLFDGETVKFD B86103A9AB5CF442 cpc_arath Transcription factor CPC Protein CAPRICE At2g46410 CPC F11C10.10 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MFRSDKAEKMDKRRRRQSKAKASCSEEVSSIEWEAVKMSEEEEDLISRMYKLVGDRWELIAGRIPGRTPEEIERYWLMKHGVVFANRRRDFFRK 608B1C7B4BA48846 myb4_arath Transcription repressor MYB4 MYB4 F20M13.180 At4g38620 Myb-related protein 4 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGRSPCCEKAHTNKGAWTKEEDERLVAYIKAHGEGCWRSLPKAAGLLRCGKSCRLRWINYLRPDLKRGNFTEEEDELIIKLHSLLGNKWSLIAGRLPGRTDNEIKNYWNTHIRRKLINRGIDPTSHRPIQESSASQDSKPTQLEPVTSNTINISFTSAPKVETFHESISFPGKSEKISMLTFKEEKDECPVQEKFPDLNLELRISLPDDVDRLQGHGKSTTPRCFKCSLGMINGMECRCGRMRCDVVGGSSKGSDMSNGFDFLGLAKKETTSLLGFRSLEMK CEFB4F1E9D8A8687 gl1_arath Trichome differentiation protein GL1 GL1 MYB0 K16N12.17 At3g27920 Protein GLABROUS 1 Protein GLABRA 1 R2R3-MYB transcription factor GL1 Myb-related protein 0 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MRIRRRDEKENQEYKKGLWTVEEDNILMDYVLNHGTGQWNRIVRKTGLKRCGKSCRLRWMNYLSPNVNKGNFTEQEEDLIIRLHKLLGNRWSLIAKRVPGRTDNQVKNYWNTHLSKKLVGDYSSAVKTTGEDDDSPPSLFITAATPSSCHHQQENIYENIAKSFNGVVSASYEDKPKQELAQKDVLMATTNDPSHYYGNNALWVHDDDFELSSLVMMNFASGDVEYCL DIP protein P27900 original sequence version: 134 822A8646F446F6B9 tt2_arath Transcription factor TT2 TT2 MYB123 At5g35550 MOK9.18 Protein TRANSPARENT TESTA 2 Myb-related protein 123 Myb-related transcription factor LBM2-like protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MGKRATTSVRREELNRGAWTDHEDKILRDYITTHGEGKWSTLPNQAGLKRCGKSCRLRWKNYLRPGIKRGNISSDEEELIIRLHNLLGNRWSLIAGRLPGRTDNEIKNHWNSNLRKRLPKTQTKQPKRIKHSTNNENNVCVIRTKAIRCSKTLLFSDLSLQKKSSTSPLPLKEQEMDQGGSSLMGDLEFDFDRIHSEFHFPDLMDFDGLDCGNVTSLVSSNEILGELVPAQGNLDLNRPFTSCHHRGDDEDWLRDFTC 3BA9CB3F723D1C2E gl3_arath Transcription factor GLABRA 3 Basic helix-loop-helix protein 1 Protein SHAPESHIFTER At5g41315 GL3 BHLH1 MYC6 SST MYC6.2 EN31 Transcription factor EN 31 bHLH transcription factor bHLH001 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MATGQNRTTVPENLKKHLAVSVRNIQWSYGIFWSVSASQSGVLEWGDGYYNGDIKTRKTIQASEIKADQLGLRRSEQLSELYESLSVAESSSSGVAAGSQVTRRASAAALSPEDLADTEWYYLVCMSFVFNIGEGMPGRTFANGEPIWLCNAHTADSKVFSRSLLAKSAAVKTVVCFPFLGGVVEIGTTEHITEDMNVIQCVKTSFLEAPDPYATILPARSDYHIDNVLDPQQILGDEIYAPMFSTEPFPTASPSRTTNGFDQEHEQVADDHDSFMTERITGGASQVQSWQLMDDELSNCVHQSLNSSDCVSQTFVEGAAGRVAYGARKSRVQRLGQIQEQQRNVKTLSFDPRNDDVHYQSVISTIFKTNHQLILGPQFRNCDKQSSFTRWKKSSSSSSGTATVTAPSQGMLKKIIFDVPRVHQKEKLMLDSPEARDETGNHAVLEKKRREKLNERFMTLRKIIPSINKIDKVSILDDTIEYLQELERRVQELESCRESTDTETRGTMTMKRKKPCDAGERTSANCANNETGNGKKVSVNNVGEAEPADTGFTGLTDNLRIGSFGNEVVIELRCAWREGVLLEIMDVISDLHLDSHSVQSSTGDGLLCLTVNCKHKGSKIATPGMIKEALQRVAWIC 5225EF0E9745CDB7 wer_arath Transcription factor WER Protein WEREWOLF Myb-related protein 66 WER MYB66 At5g14750 T9L3.50 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MRKKVSSSGDEGNNEYKKGLWTVEEDKILMDYVKAHGKGHWNRIAKKTGLKRCGKSCRLRWMNYLSPNVKRGNFTEQEEDLIIRLHKLLGNRWSLIAKRVPGRTDNQVKNYWNTHLSKKLGIKDQKTKQSNGDIVYQINLPNPTETSEETKISNIVDNNNILGDEIQEDHQGSNYLSSLWVHEDEFELSTLTNMMDFIDGHCF EFAB8A342F0FB66F tt8_arath Transcription factor TT8 TT8 BHLH42 Basic helix-loop-helix protein 42 EN32 Transcription factor EN 32 Protein TRANSPARENT TESTA 8 bHLH transcription factor bHLH042 F17A8.170 At4g09820 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MDESSIIPAEKVAGAEKKELQGLLKTAVQSVDWTYSVFWQFCPQQRVLVWGNGYYNGAIKTRKTTQPAEVTAEEAALERSQQLRELYETLLAGESTSEARACTALSPEDLTETEWFYLMCVSFSFPPPSGMPGKAYARRKHVWLSGANEVDSKTFSRAILAKSAKIQTVVCIPMLDGVVELGTTKKVREDVEFVELTKSFFYDHCKTNPKPALSEHSTYEVHEEAEDEEEVEEEMTMSEEMRLGSPDDEDVSNQNLHSDLHIESTHTLDTHMDMMNLMEEGGNYSQTVTTLLMSHPTSLLSDSVSTSSYIQSSFATWRVENGKEHQQVKTAPSSQWVLKQMIFRVPFLHDNTKDKRLPREDLSHVVAERRRREKLNEKFITLRSMVPFVTKMDKVSILGDTIAYVNHLRKRVHELENTHHEQQHKRTRTCKRKTSEEVEVSIIENDVLLEMRCEYRDGLLLDILQVLHELGIETTAVHTSVNDHDFEAEIRAKVRGKKASIAEVKRAIHQVIIHDTNL 25988482FE25C99C my114_arath Transcription factor MYB114 MYB114 At1g66380 Myb-related protein 114 T27F4.13 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MEGSSKGLRKGAWTAEEDSLLRQCIGKYGEGKWHQVPLRAGLNRCRKSCRLRWLNYLKPSIKRGKFSSDEVDLLLRLHKLLGNRWSLIAGRLPGRTANDVKNYWNTHLSKKHEPCCKTKIKRINIITPPNTPAQKVDIF 81D7B545F8274461 myb90_arath Transcription factor MYB90 MYB90 PAP2 T27F4.14 At1g66390 Myb-related protein 90 Production of anthocyanin pigment 2 protein protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MEGSSKGLRKGAWTAEEDSLLRLCIDKYGEGKWHQVPLRAGLNRCRKSCRLRWLNYLKPSIKRGRLSNDEVDLLLRLHKLLGNRWSLIAGRLPGRTANDVKNYWNTHLSKKHESSCCKSKMKKKNIISPPTTPVQKIGVFKPRPRSFSVNNGCSHLNGLPEVDLIPSCLGLKKNNVCENSITCNKDDEKDDFVNNLMNGDNMWLENLLGENQEADAIVPEATTAEHGATLAFDVEQLWSLFDGETVELD 309024FD4103700A egl3-pap1 2 11 unspecified role unspecified role bait bait 12 unspecified role unspecified role prey prey physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). egl3-pap2 2 11 unspecified role unspecified role bait bait 21 unspecified role unspecified role prey prey physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). egl3-myb113 2 4 unspecified role unspecified role prey prey 11 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). egl3-myb114 2 20 unspecified role unspecified role prey prey 11 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). egl3-myb5 2 11 unspecified role unspecified role bait bait 6 unspecified role unspecified role prey prey physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). egl3-tt2 2 16 unspecified role unspecified role prey prey 11 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). egl3-gl1 2 15 unspecified role unspecified role prey prey 11 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). egl3-myb23 2 5 unspecified role unspecified role prey prey 11 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 3 millimolar 3-AT (3-amino-1,2,4-triazole). egl3-wer-1 2 18 unspecified role unspecified role prey prey 11 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 3 millimolar 3-AT (3-amino-1,2,4-triazole). bhlh012-pap1 2 12 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). bhlh012-pap2 2 7 unspecified role unspecified role bait bait 21 unspecified role unspecified role prey prey physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). bhlh012-myb113 2 7 unspecified role unspecified role bait bait 4 unspecified role unspecified role prey prey physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). bhlh012-myb114 2 20 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). bhlh012-myb5 2 7 unspecified role unspecified role bait bait 6 unspecified role unspecified role prey prey physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). bhlh012-tt2-1 2 7 unspecified role unspecified role bait bait 16 unspecified role unspecified role prey prey physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). bhlh012-gl1 2 15 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). bhlh012-myb23 2 5 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 3 millimolar 3-AT (3-amino-1,2,4-triazole). bhlh012-wer-2 2 18 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 3 millimolar 3-AT (3-amino-1,2,4-triazole). tt8-pap1-1 2 12 unspecified role unspecified role prey prey 19 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). tt8-pap2-2 2 19 unspecified role unspecified role bait bait 21 unspecified role unspecified role prey prey physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). tt8-myb113-1 2 4 unspecified role unspecified role prey prey 19 unspecified role unspecified role bait bait physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 3 millimolar 3-AT (3-amino-1,2,4-triazole). tt8-myb114 2 19 unspecified role unspecified role bait bait 20 unspecified role unspecified role prey prey physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 3 millimolar 3-AT (3-amino-1,2,4-triazole). tt8-myb5 2 19 unspecified role unspecified role bait bait 6 unspecified role unspecified role prey prey physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 20 millimolar 3-AT (3-amino-1,2,4-triazole). tt8-tt2 2 19 unspecified role unspecified role bait bait 16 unspecified role unspecified role prey prey physical association physical association 1a 1b EGL3, AtBHLH012 and TT8 consistently activated both reporters when cotransformed with AtMYB5, with the MYB proteins of subgroup 5 (PAP1, PAP2, AtMYB113 and AtMYB114) and with TT2 (subgroup 6), respectively. In contrast, MYB proteins from subgroup 15 (GL1, WER, AtMYB23) interacted with EGL3 and AtBHLH012 but not with TT8 (Figure 1a,b). Colony growth at 3 millimolar 3-AT (3-amino-1,2,4-triazole). pap1-egl3 3 12 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 11 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro physical association physical association 1c IIIf including GL3 (data not shown). Selected interactions were confirmed by in vitro pulldown assays. GST-tagged PAP1 and PAP2, respectively, was purified from Escherichia coli and bound to GSH agarose beads. As a negative control beads were loaded with GST. The loaded beads were incubated with in vitro translated and radioactively labelled GL3, EGL3, TT8, AtBHLH012 and AtBHLH013, respectively. Both, PAP1 and PAP2, specifically interacted in vitro with all four R/B-like BHLH proteins from subgroup IIIf. No binding of the related AtBHLH013 from subgroup IIIe was detected, confirming the results of the yeast two-hybrid assays (Figure 1c). pap2-egl3-1 3 11 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro 21 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) physical association physical association 1c IIIf including GL3 (data not shown). Selected interactions were confirmed by in vitro pulldown assays. GST-tagged PAP1 and PAP2, respectively, was purified from Escherichia coli and bound to GSH agarose beads. As a negative control beads were loaded with GST. The loaded beads were incubated with in vitro translated and radioactively labelled GL3, EGL3, TT8, AtBHLH012 and AtBHLH013, respectively. Both, PAP1 and PAP2, specifically interacted in vitro with all four R/B-like BHLH proteins from subgroup IIIf. No binding of the related AtBHLH013 from subgroup IIIe was detected, confirming the results of the yeast two-hybrid assays (Figure 1c). pap1-gl3 3 17 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro 12 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) physical association physical association 1c Selected interactions were confirmed by in vitro pulldown assays. GST-tagged PAP1 and PAP2, respectively, was purified from Escherichia coli and bound to GSH agarose beads. As a negative control beads were loaded with GST. The loaded beads were incubated with in vitro translated and radioactively labelled GL3, EGL3, TT8, AtBHLH012 and AtBHLH013, respectively. Both, PAP1 and PAP2, specifically interacted in vitro with all four R/B-like BHLH proteins from subgroup IIIf. No binding of the related AtBHLH013 from subgroup IIIe was detected, confirming the results of the yeast two-hybrid assays (Figure 1c). pap2-gl3-2 3 17 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro 21 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) physical association physical association 1c Selected interactions were confirmed by in vitro pulldown assays. GST-tagged PAP1 and PAP2, respectively, was purified from Escherichia coli and bound to GSH agarose beads. As a negative control beads were loaded with GST. The loaded beads were incubated with in vitro translated and radioactively labelled GL3, EGL3, TT8, AtBHLH012 and AtBHLH013, respectively. Both, PAP1 and PAP2, specifically interacted in vitro with all four R/B-like BHLH proteins from subgroup IIIf. No binding of the related AtBHLH013 from subgroup IIIe was detected, confirming the results of the yeast two-hybrid assays (Figure 1c). pap2-bhlh012 3 7 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro 21 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) physical association physical association 1c Selected interactions were confirmed by in vitro pulldown assays. GST-tagged PAP1 and PAP2, respectively, was purified from Escherichia coli and bound to GSH agarose beads. As a negative control beads were loaded with GST. The loaded beads were incubated with in vitro translated and radioactively labelled GL3, EGL3, TT8, AtBHLH012 and AtBHLH013, respectively. Both, PAP1 and PAP2, specifically interacted in vitro with all four R/B-like BHLH proteins from subgroup IIIf. No binding of the related AtBHLH013 from subgroup IIIe was detected, confirming the results of the yeast two-hybrid assays (Figure 1c). pap1-bhlh012 3 12 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro physical association physical association 1c Selected interactions were confirmed by in vitro pulldown assays. GST-tagged PAP1 and PAP2, respectively, was purified from Escherichia coli and bound to GSH agarose beads. As a negative control beads were loaded with GST. The loaded beads were incubated with in vitro translated and radioactively labelled GL3, EGL3, TT8, AtBHLH012 and AtBHLH013, respectively. Both, PAP1 and PAP2, specifically interacted in vitro with all four R/B-like BHLH proteins from subgroup IIIf. No binding of the related AtBHLH013 from subgroup IIIe was detected, confirming the results of the yeast two-hybrid assays (Figure 1c). pap1-tt8 3 19 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro 12 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) physical association physical association 1c Selected interactions were confirmed by in vitro pulldown assays. GST-tagged PAP1 and PAP2, respectively, was purified from Escherichia coli and bound to GSH agarose beads. As a negative control beads were loaded with GST. The loaded beads were incubated with in vitro translated and radioactively labelled GL3, EGL3, TT8, AtBHLH012 and AtBHLH013, respectively. Both, PAP1 and PAP2, specifically interacted in vitro with all four R/B-like BHLH proteins from subgroup IIIf. No binding of the related AtBHLH013 from subgroup IIIe was detected, confirming the results of the yeast two-hybrid assays (Figure 1c). pap2-tt8 3 21 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 19 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro physical association physical association 1c Selected interactions were confirmed by in vitro pulldown assays. GST-tagged PAP1 and PAP2, respectively, was purified from Escherichia coli and bound to GSH agarose beads. As a negative control beads were loaded with GST. The loaded beads were incubated with in vitro translated and radioactively labelled GL3, EGL3, TT8, AtBHLH012 and AtBHLH013, respectively. Both, PAP1 and PAP2, specifically interacted in vitro with all four R/B-like BHLH proteins from subgroup IIIf. No binding of the related AtBHLH013 from subgroup IIIe was detected, confirming the results of the yeast two-hybrid assays (Figure 1c). bhlh012-mybl2 1 7 unspecified role unspecified role bait bait 8 unspecified role unspecified role prey prey physical association physical association four 1R MYB proteins (AtMYBL2, CPC, At1g01380 and At2g30420) were identified in screenings using AtBHLH012 as bait protein. bhlh012-at1g01380 1 7 unspecified role unspecified role bait bait 10 unspecified role unspecified role prey prey physical association physical association four 1R MYB proteins (AtMYBL2, CPC, At1g01380 and At2g30420) were identified in screenings using AtBHLH012 as bait protein. bhlh012-at2g30420 1 9 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait physical association physical association four 1R MYB proteins (AtMYBL2, CPC, At1g01380 and At2g30420) were identified in screenings using AtBHLH012 as bait protein. bhlh012-cpc 1 7 unspecified role unspecified role bait bait 13 unspecified role unspecified role prey prey physical association physical association four 1R MYB proteins (AtMYBL2, CPC, At1g01380 and At2g30420) were identified in screenings using AtBHLH012 as bait protein. egl3-mybl2 1 8 unspecified role unspecified role prey prey 11 unspecified role unspecified role bait bait physical association physical association Furthermore, AtMYBL2 and the CPC-homologue At1g01380 were isolated in screenings using EGL3 as bait. egl3-at1g01380 1 11 unspecified role unspecified role bait bait 10 unspecified role unspecified role prey prey physical association physical association Furthermore, AtMYBL2 and the CPC-homologue At1g01380 were isolated in screenings using EGL3 as bait. tt8-mybl2 1 8 unspecified role unspecified role prey prey 19 unspecified role unspecified role bait bait physical association physical association Additionally, CPC and AtMYBL2 were detected with TT8 as bait. tt8-cpc 1 13 unspecified role unspecified role prey prey 19 unspecified role unspecified role bait bait physical association physical association Additionally, CPC and AtMYBL2 were detected with TT8 as bait. bhlh012-pap1-1 2 7 unspecified role unspecified role bait bait 12 unspecified role unspecified role prey prey region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain physical association physical association 3 Protein fragments were fused to the GAL4-AD and tested for interaction with the set of AtBHLH transcription factors. The minimal domain necessary for interaction was confined to amino acids 53 to 114 comprising accurately the complete R3-repeat of the MYB domain of PAP1. It is clear from Figure 3 that the region 100 - 114 amino acid residues is able to interact with the bait protein and form the minimum unit of interaction; the authors conclude that the regions required is 53 - 114 amino acids residues. egl3-pap1-1 2 12 unspecified role unspecified role prey prey 11 unspecified role unspecified role bait bait physical association physical association 3 Protein fragments were fused to the GAL4-AD and tested for interaction with the set of AtBHLH transcription factors. The minimal domain necessary for interaction was confined to amino acids 53 to 114 comprising accurately the complete R3-repeat of the MYB domain of PAP1. It is clear from Figure 3 that the region 100 - 114 amino acid residues is able to interact with the bait protein and form the minimum unit of interaction; the authors conclude that the regions required is 53 - 114 amino acids residues. bhlh012-cpc-1 2 7 unspecified role unspecified role bait bait 13 unspecified role unspecified role prey prey region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association The shortest 1R MYB proteins identified were CPC consisting of amino acids 37�94 3 egl3-cpc-2 2 11 unspecified role unspecified role bait bait 13 unspecified role unspecified role prey prey region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association The shortest 1R MYB proteins identified were CPC consisting of amino acids 37�94 3 bhlh012-at1g01380-1 2 7 unspecified role unspecified role bait bait 10 unspecified role unspecified role prey prey region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association 3 Protein fragments were fused to the GAL4-AD and tested for interaction with the set of AtBHLH transcription factors. The minimal domain necessary for interaction was confined to amino acids 53 to 114 comprising accurately the complete R3-repeat of the MYB domain of PAP1. These findings were supported by the fact that, from the library screenings, several N-terminally truncated MYB proteins have been isolated. The shortest 1R MYB proteins identified were CPC consisting of amino acids 37�94 and the CPC-homologue At1g01380 comprising amino acids 33�83, respectively (Figure 3). egl3-at1g01380-1 2 10 unspecified role unspecified role prey prey region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 11 unspecified role unspecified role bait bait physical association physical association 3 Protein fragments were fused to the GAL4-AD and tested for interaction with the set of AtBHLH transcription factors. The minimal domain necessary for interaction was confined to amino acids 53 to 114 comprising accurately the complete R3-repeat of the MYB domain of PAP1. These findings were supported by the fact that, from the library screenings, several N-terminally truncated MYB proteins have been isolated. The shortest 1R MYB proteins identified were CPC consisting of amino acids 37�94 and the CPC-homologue At1g01380 comprising amino acids 33�83, respectively (Figure 3). egl3-pap1-2 2 11 unspecified role unspecified role bait bait 12 unspecified role unspecified role prey prey Q9FE25:p.Leu73Ile mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L I Wed May 02 16:32:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu73ile' Tue Jun 30 16:04:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu73Ile' Q9FE25:p.Arg76Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R E Wed May 02 15:18:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg76glu' Tue Jun 30 20:12:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg76Glu' Q9FE25:p.Arg76Lys mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R K Wed May 02 16:44:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg76lys' Tue Jun 30 19:59:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg76Lys' Q9FE25:p.Arg79Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R S Wed May 02 15:31:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg79ser' Tue Jun 30 16:39:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg79Ser' Q9FE25:p.Leu80Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L A Wed May 02 18:24:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu80ala' Tue Jun 30 16:43:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu80Ala' Q9FE25:p.Arg91Asp mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R D Wed May 02 20:10:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg91asp' Tue Jun 30 16:32:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg91Asp' Q9FE25:p.Arg91Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain R A Wed May 02 18:28:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg91ala' Tue Jun 30 18:27:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg91Ala' physical association physical association 7a In addition to mutations D12N, L20V and L29I obtained by the randommutagenesis approach, the single-site mutants L13I, R16E, R16K, R19S, L20A, R33D and R33A were analysed. With the exception of R19S, all of these exchanges led to temperature- sensitive interaction with EGL3, revealed by reduced growth of yeast cells at non-permissive temperatures. Quantification of the interaction strength by liquid alpha-galactosidase assays demonstrated that exchanges at positions 73 and 76 had no or only a minor impact on the interaction, whereas mutation of either amino acid position 80 or 91 strongly decreased the interaction bhlh012-myb4 2 14 unspecified role unspecified role prey prey n-terminal required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 7 unspecified role unspecified role bait bait physical association physical association 8 Deletion of the entire C-terminal region (AtMYB4_1-118) resulted in strong interaction with BHLH012 and weaker but significant interaction with TT8. tt8-myb4-1 2 14 unspecified role unspecified role prey prey n-terminal required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 19 unspecified role unspecified role bait bait physical association physical association 8 Deletion of the entire C-terminal region (AtMYB4_1-118) resulted in strong interaction with BHLH012 and weaker but significant interaction with TT8. The authors note that there was weaker but significant interaction between MYB4 and TT8 proteins.