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/ AtTRP1 encodes a novel TPR protein that interacts with the ethylene receptor ERS1 and modulates development in Arabidopsis. AtTRP1 encodes a novel TPR protein that interacts with the ethylene receptor ERS1 and modulates development in Arabidopsis. J. Exp. Bot. (0022-0957) 2009 imex curation Lin Z., Ho C.W., Grierson D. donald.grierson@nottingham.ac.uk orchard Only protein-protein interactions 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 Lin Z., Ho C.W., Grierson D. donald.grierson@nottingham.ac.uk Accepted 2009-SEP-7 by ORCHARD. J. Exp. Bot. (0022-0957) 2009 orchard Only protein-protein interactions imex curation AtTRP1 encodes a novel TPR protein that interacts with the ethylene receptor ERS1 and modulates development in Arabidopsis. AtTRP1 encodes a novel TPR protein that interacts with the ethylene receptor ERS1 and modulates development in Arabidopsis. J. Exp. Bot. (0022-0957) 2009 imex curation Lin Z., Ho C.W., Grierson D. donald.grierson@nottingham.ac.uk orchard Only protein-protein interactions arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Lin Z., Ho C.W., Grierson D. Transgenic Arabidopsis plants expressing GFP tagged TRP1 protein construct were used in this assay. donald.grierson@nottingham.ac.uk Accepted 2009-SEP-7 by ORCHARD. J. Exp. Bot. (0022-0957) 2009 orchard Only protein-protein interactions imex curation etr1_sollc Ethylene receptor 1 ETR1 protein protein sollc Solanum lycopersicum (Tomato) Lycopersicon esculentum Tomato MGSLLRMNRLLSSIVESCNCIIDPQLPADDLLMKYQYISDFFIALAYFSIPVELIYFVKKSAVFPYRWVLVQFGAFIVLCGATHLINLWTFNMHTRNVAIVMTTPKALTALVSCITALMLVHIIPDLLSVKTRELFLKKKAAQLDREMGIIRTQEETGRHVRMLTHEIRSTLDRHTILKTTLVELGRTLALEECALWMPTRTGLELQLSYTLRHQNPVGLTVPIQLPVINQVFGTNHVVKISPNSPVARLRPAGKYMPGEVVAVRVPLLHLSNFQINDWPELSTKRYALMVLMLPSDSARQWHVHELELVEVVADQVAVALSHAAILEESMRARDLLMEQNVALDLARREAEMAVRARNDFLAVMNHEMRTPMHAIIALSSLLQETDLTPEQRLMVETILKSSNLLATLINDVLDLSRLEDGSLQLDIGTFNLHALFREVHSLIKPIASVKKLFVTLSLSSDLPEYVIGDEKRLMQILLNVVGNAVKFSKEGNVSISAFVAKSDSLRDPRAPEFFAVPSENHFYLRVQIKDTGIGITPQDIPNLFSKFTQSQALATTNSGGTGLGLAICKRFVNLMEGHIWIESEGLGKGSTAIFIIKLGIPGRANESKLPFVTKLPANHTQMSFQGLKVLVMDENGVSRMVTKGLLTHLGCDVTTVGSRDECLRVVTHEHKVVIMDVSMQGIDCYEVAVVIHERFGKRHGRPLIVALTGNTDRVTKENCMRVGMDGVILKPVSVYKMRSVLSELLEHGVVLES D7443B6517781D0A q41341_sollc Never-ripe ETR3 544279 protein protein sollc Solanum lycopersicum (Tomato) Lycopersicon esculentum Tomato MESCDCIEALLPTGDLLVKYQYLSDFFIAVAYFSIPLELIYFVHKSACFPYRWVLMQFGAFIVLCGATHFISLWTFFMHSKTVAVVMTISKMLTAAVSCITALMLVHIIPDLLSVKTRELFLKTRAEELDKEMGLIIRQEETGRHVRMLTHEIRSTLDRHTILKTTLVELGRTLDLAECALWMPCQGGLTLQLSHNLNNLIPLGSTVPINLPIINEIFSSPEAIQIPHTNPLARMRNTVGRYIPPEVVAVRVPLLHLSNFTNDWAELSTRSYAVMVLVLPMNGLRKWREHELELVQVVADQVAVALSHAAILEDSMRAHDQLMEQNIALDVARQEAEMAIRARNDFLAVMNHEMRTPMHAVIALCSLLLETDLTPEQRVMIETILKSSNLLATLINDVLDLSRLEDGILELENGTFNLHGILREAVNLIKPIASLKKLSITLALALDLPILAVGDAKRLIQTLLNVAGNAVKFTKEGHISIEASVAKPEYARDCHPPEMFPMPSDGQFYLRVQVRDTGCGISPQDIPLVFTKFAESRPTSNRSTGGEGLGLAICRRFIQLMKGNIWIESEGPGKGTTVTFVVKLGICHHPNALPLLPMPPRGRLNKGSDDLFRYRQFRGDDGGMSVNAQRYQRSL 40E40D2858EB170C ers1_arath Ethylene response sensor 1 ERS1 ERS At2g40940 Protein ERS1 T20B5.14 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MESCDCFETHVNQDDLLVKYQYISDALIALAYFSIPLELIYFVQKSAFFPYKWVLMQFGAFIILCGATHFINLWMFFMHSKAVAIVMTIAKVSCAVVSCATALMLVHIIPDLLSVKNRELFLKKKADELDREMGLILTQEETGRHVRMLTHGIRRTLDRHTILRTTLVELGKTLCLEECALWMPSQSGLYLQLSHTLSHKIQVGSSVPINLPIINELFNSAQAMHIPHSCPLAKIGPPVGRYSPPEVVSVRVPLLHLSNFQGSDWSDLSGKGYAIMVLILPTDGARKWRDHELELVENVADQVAVALSHAAILEESMHARDQLMEQNFALDKARQEAEMAVHARNDFLAVMNHEMRTPMHAIISLSSLLLETELSPEQRVMIETILKSSNLVATLISDVLDLSRLEDGSLLLENEPFSLQAIFEEVISLIKPIASVKKLSTNLILSADLPTYAIGDEKRLMQTILNIMGNAVKFTKEGYISIIASIMKPESLQELPSPEFFPVLSDSHFYLCVQVKDTGCGIHTQDIPLLFTKFVQPRTGTQRNHSGGGLGLALCKRFVGLMGGYMWIESEGLEKGCTASFIIRLGICNGPSSSSGSMALHLAAKSQTRPWNW E4F5DB384E6727B2 trp1_arath Telomere repeat-binding protein 1 TRP1 F2O15.20 At5g59430 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MVSHKCVEEFGYASYLVPSNARAPRSARKRRSIEKRISKEDDNMCAIDLLATVAGHLSFESGSSLMSIDKLIEDHRVKEEFPEEEKPLMPVALSPYRGSLSPCGFSSVINGKVENEVDGFSYSGGSDACQVGNFSQDVKPDIDGDAVVLDARPNVVVSLGSSSRTEVPSIGNCVSHGVRDDVNLFSRDDDENFSKYIHPRVTKHSPRTVPRIGDRRIRKILASRHWKGGSRHSDTKPWRNYYLHQQRSYPIKKRKNFDHISDSVTDDYRMRTKMHRGSRKGQGASFVASDSHVKLRIKSFRVPELFIEIPETATVGSLKRMVMEAVSTLLSDGHRVGLMVQGKKVRDDNKTLHQTGISQDNSHLDSLDFSLEPSSEMPQLLTSHPLGHACEELLPVCQATKIDNVLESDHHDSALFPSDSLGNNNVTEDSKAMISVALNELSSQSQPPSRKSRRSEQQQQQAAQRRIRRPFSVAEVEALVQAVEKLGTGRWRDVKLCAFEDADHRTYVDLKDKWKTLVHTAKISPQQRRGEPVPQELLNRVLNAHGYWTQQQMQQLQQNVNKLEQETQSQTTEGLLLL 853B54C5FC2E5E01 trp1-esr1 1 6 unspecified role unspecified role bait bait 5 unspecified role unspecified role prey prey c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association Figure 9C The interaction assays showed that AtTRP1 interacted with ERS1 and not with ETR1, whereas the prey vector pJG4-5 caused no interaction with either receptor trp1-etr1 1 6 unspecified role unspecified role bait bait 3 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association Figure 9C The interactions of AtTPR1 with the tomato ethylene receptors NR and LeETR1 were also examined. The NR partial cDNA encoding the NR protein without the transmembrane domain (NR117-635), together with the two partial cDNAs of LeETR1 encoding either the LeETR1 protein lacking the transmembrane domain (LeETR1132-754) or the histidine kinase domain alone (LeETR1364-647) were cloned into the bait vector pEG202 downstream of the LexA DNA-binding domain (DB) (Fig. 9B) (Lin et al., 2008c). All three tomato receptor constructs were shown to interact with AtTRP1 in yeast trp1-etr3 1 6 unspecified role unspecified role bait bait 4 unspecified role unspecified role prey prey c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain physical association physical association Figure 9C The interactions of AtTPR1 with the tomato ethylene receptors NR and LeETR1 were also examined. The NR partial cDNA encoding the NR protein without the transmembrane domain (NR117-635), together with the two partial cDNAs of LeETR1 encoding either the LeETR1 protein lacking the transmembrane domain (LeETR1132-754) or the histidine kinase domain alone (LeETR1364-647) were cloned into the bait vector pEG202 downstream of the LexA DNA-binding domain (DB) (Fig. 9B) (Lin et al., 2008c). All three tomato receptor constructs were shown to interact with AtTRP1 in yeast trp1-etr3-1 2 6 unspecified role unspecified role bait bait region gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 5 unspecified role unspecified role prey prey physical association physical association Figure 9E When the immunoprecipitated samples were challenged with the anti-NR antibody, the results showed that the ERS1 protein was co-immunoprecipitated with the AtTPR1�GFP protein as homodimers and no monomers were detected The authors concluded that the anti-NR antibody used in the study detected the Arabidopsis ESR1 protein. Furthermore, "the ERS1 protein was co-immunoprecipitated with the AtTPR1-GFP protein as homodimers and no monomers were detected".