DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252757X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252768X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions in vitro In vitro anti tag coip anti tag coimmunoprecipitation anti tag coip weight by comassie molecular weight estimation by coomasie staining weight by comassie Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252765X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252759X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252756X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions in vitro In vitro anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252763X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions in vitro In vitro anti tag coip anti tag coimmunoprecipitation anti tag coip weight by comassie molecular weight estimation by coomasie staining weight by comassie Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252766X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252767X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions in vitro In vitro anti tag coip anti tag coimmunoprecipitation anti tag coip weight silver stain molecular weight estimation by silver staining weight silver stain Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252760X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252762X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252758X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions in vitro In vitro anti tag coip anti tag coimmunoprecipitation anti tag coip weight silver stain molecular weight estimation by silver staining weight silver stain Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252764X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. Nature 2013 imex curation Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Hondele M., Stuwe T., Hassler M., Halbach F., Bowman A., Zhang ET., Nijmeijer B., Kotthoff C., Rybin V., Amlacher S., Hurt E., Ladurner AG. DIP original experiment: DIP-252761X Nature 2013 IMEx Structural basis of histone H2A-H2B recognition by the essential chaperone FACT. g0sdn1_chatd FACT complex subunit CTHT_0052370 protein protein chatd Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) MADIKIDSKLFQERISHFISAWKADKRSGDALFGGVSSIVILMGKVDEEPEFYKNNAMHFWLLGYEFPTTLMLFTLDTLYIITTQKKAKYLDQIKGGRFPVEVLVRGKDNAENEKTFIKIADMIKAAGNKVGVLTKDTSKGPFIDEWKKIFAERCKGVEEVDIALALSAGAFSIKDETELRAMRTSSKACVALLTPYFLDEMSSILDQDKKISHASLADKVMNKLEDEKFWKTVELPNRGKLPSDFDPEQLDWILGPIVQSGGKFDLKWQTDSDDEPLHPGIIIAAMGLRYKSYCSQIARTFMVDPNKSQESNYRVLLAVHNLILKEIRDGVVVKDVYNKAYNLIKTKKPELEKHFLKNVGYGIGLESKDSTLILSAKNTRTLKDGMTLCIVTGFSDIPNPDPQGKKDKVYSLVLTDTIRVTTGEPVVFTGEAPSDMDATSFFFKDEEEAQPTPKKEKKDPRVGAVATRNITSTRLRSERNTAPDEDAEKRRREHQKELAAKKQKEGLLKYADATAGQNGVEVKKFKRFESYKRDNQLPPKVRDMGIVIDQKNNTIVLPIMGRPVPFHINTIKNASKSDEGEWSFLRINFLSPGQGVGRKDDQPFEDASAHFVRSLTFRSTDGDRYAEIANQISNLKREAVKREQEKKDLEDVVEQDKLIEIRNRRPAVLDNVYIRPALEGKRVPGKVEIHQNGIRYQSPLSTTQRVDVLFSNIRHLFFQPCQNEMIVIIHLHLKDPILFGKKKTKDVQFYREAIDIQFDETGNRKRKYRYGDEDEFEAEQEERRRKAELDRLFKSFAEKIAEAGRNEGIEVDMPIRDLGFNGVPNRSNVVIYPTTECLIQITEPPFLVITLEDVEWAHLERVQFGLKNFDLVFVFKDFTRPVVHINTIPVESLEDVKEFLDSSDIPFSEGPLNLNWSVIMKTVTANPHQFFLDGGWGFLQNDSDASDASEEEEDEDSAFEISESELEAASESSEEDSDYEDASEEESDAPPSEDDEGESWDELERKARKRDRESGLDDDDRGGKKRRR DIP protein G0SDN1 original sequence version: 7 q92133_xenla Histone H3 h3c8.S H3l h3c8 hist1h3g protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCGIHAKRVTIMPKDIQLARRIRGERA DIP protein Q92133 original sequence version: 87 69B8368EA50A0EEC dpoa_yeast DNA polymerase alpha catalytic subunit A POL1 CDC17 DNA polymerase alpha:primase complex p180 subunit DNA polymerase I subunit A N2181 YNL102W protein protein yeast Saccharomyces cerevisiae Baker's yeast MSSKSEKLEKLRKLQAARNGTSIDDYEGDESDGDRIYDEIDEKEYRARKRQELLHDDFVVDDDGVGYVDRGVEEDWREVDNSSSDEDTGNLASKDSKRKKNIKREKDHQITDMLRTQHSKSTLLAHAKKSQKKSIPIDNFDDILGEFESGEVEKPNILLPSKLRENLNSSPTSEFKSSIKRVNGNDESSHDAGISKKVKIDPDSSTDKYLEIESSPLKLQSRKLRYANDVQDLLDDVENSPVVATKRQNVLQDTLLANPPSAQSLADEEDDEDSDEDIILKRRTMRSVTTTRRVNIDSRSNPSTSPFVTAPGTPIGIKGLTPSKSLQSNTDVATLAVNVKKEDVVDPETDTFQMFWLDYCEVNNTLILFGKVKLKDDNCVSAMVQINGLCRELFFLPREGKTPTDIHEEIIPLLMDKYGLDNIRAKPQKMKYSFELPDIPSESDYLKVLLPYQTPKSSRDTIPSDLSSDTFYHVFGGNSNIFESFVIQNRIMGPCWLDIKGADFNSIRNASHCAVEVSVDKPQNITPTTTKTMPNLRCLSLSIQTLMNPKENKQEIVSITLSAYRNISLDSPIPENIKPDDLCTLVRPPQSTSFPLGLAALAKQKLPGRVRLFNNEKAMLSCFCAMLKVEDPDVIIGHRLQNVYLDVLAHRMHDLNIPTFSSIGRRLRRTWPEKFGRGNSNMNHFFISDICSGRLICDIANEMGQSLTPKCQSWDLSEMYQVTCEKEHKPLDIDYQNPQYQNDVNSMTMALQENITNCMISAEVSYRIQLLTLTKQLTNLAGNAWAQTLGGTRAGRNEYILLHEFSRNGFIVPDKEGNRSRAQKQRQNEENADAPVNSKKAKYQGGLVFEPEKGLHKNYVLVMDFNSLYPSIIQEFNICFTTVDRNKEDIDELPSVPPSEVDQGVLPRLLANLVDRRREVKKVMKTETDPHKRVQCDIRQQALKLTANSMYGCLGYVNSRFYAKPLAMLVTNKGREILMNTRQLAESMNLLVVYGDTDSVMIDTGCDNYADAIKIGLGFKRLVNERYRLLEIDIDNVFKKLLLHAKKKYAALTVNLDKNGNGTTVLEVKGLDMKRREFCPLSRDVSIHVLNTILSDKDPEEALQEVYDYLEDIRIKVETNNIRIDKYKINMKLSKDPKAYPGGKNMPAVQVALRMRKAGRVVKAGSVITFVITKQDEIDNAADTPALSVAERAHALNEVMIKSNNLIPDPQYYLEKQIFAPVERLLERIDSFNVVRLSEALGLDSKKYFRREGGNNNGEDINNLQPLETTITDVERFKDTVTLELSCPSCDKRFPFGGIVSSNYYRVSYNGLQCKHCEQLFTPLQLTSQIEHSIRAHISLYYAGWLQCDDSTCGIVTRQVSVFGKRCLNDGCTGVMRYKYSDKQLYNQLLYFDSLFDCEKNKKQELKPIYLPDDLDYPKEQLTESSIKALTEQNRELMETGRSVVQKYLNDCGRRYVDMTSIFDFMLN 50C9032DBE95B5AE 50C9032DBE95B5AE h4_xenla Histone H4 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG DIP protein P62799 original sequence version: 90 DIP protein P62799 original sequence version: 50 DIP protein P62799 original sequence version: 53 DIP protein P62799 original sequence version: 68 DIP protein P62799 original sequence version: 91 DIP protein P62799 original sequence version: 109 A9E5DFD3F8B97598 g0shk5_chatd FACT complex subunit POB3 CTHT_0070340 protein protein chatd Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) MAAIESFDHIYLDLSKEPGKCRFAENGLGWKPVGGGETFTLDVSNIGGAQWSRAARGYEVKILQRTSGVIQLDGFQQEDYERLAKIFKNWYSTNLENKEHSLRGWNWGKAEFGKAELTFNVQNRPAFEIPYSEIANTNLAGRNEIAVEFAPGDHGKSSQNGQVKSKKASASRDQLVEIRFYIPGTTTRKEAEGGEAGSDADEEEKNAVTLFYDTLIEKAEIGETAGDTIATFLDVLHLTPRGRFDIDMYDTSFRLRGKTYDYKIQYEAIKKFMVLPKPDDLHFMLCIGLDPPLRQGQTRYPFIVMQFKQDEEVTLDLNLSEEELNGKYKDRLQAHYEQPAHQVVTYIFKGLANKKVTAPAKDFTTHRGHYGIKCSIKASEGFLYCLEKAFMFVPKPATYISYEQTQSVTFSRVGGAVSTLSTFDITVHMKNGQGSSQFSNINREELKALEDFFKLKGLKVKNEIDEDANLLAAALRDDDMASSDEDVVGGKADRGSADEDEESVDEDFQAESESEVAEEYDSQHESSGSGSDEDDDDLDDDVVDDDEDEEEEEEEEEEEEEERPKKKKKTG DIP protein G0SHK5 original sequence version: 6 h2b(1130) Histone H2B peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) GSKKAVTKTQKKDGKKRRKT h2b(2648) Histone H2B peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RKTRKESYAIYVYKVLKQVHPD h3(4665) Histone H3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) VALREIRRYQKSTELLIRKL h3tail H3 tail peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ARTKQTARKSTGGKAPRKQL g0sdn1_chatd-h4_xenla-1 2 17 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role Region 651-944 Region 651-944 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association g0shk5_chatd-g0sdn1_chatd-1 5 14 unspecified role unspecified role prey prey Region 521-651 Region 521-651 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 18 unspecified role unspecified role bait bait Region 1-192 Region 1-192 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association g0sdn1_chatd-h2b(1130)-1 9 19 unspecified role unspecified role prey prey in vitro In vitro 14 unspecified role unspecified role bait bait Region 651-944 Region 651-944 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain G0SDN1:p.[Asp902Ala;Ser903Ala;Asp905Ala] D902A/S903A/D905A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain D A certain certain sequence position certain certain certain sequence position certain S A certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D902A/S903A/D905A'. Wed May 02 15:34:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp902ala,ser903ala,asp905ala' Tue Jun 30 16:02:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asp902Ala;Ser903Ala;Asp905Ala]' V5-tag V5-tag v5 tag v5 tag GKPIPNPLLGLDST epitope tag GKPIPNPLLGLDST epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction h4_xenla-hist1h3g-1 8 17 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction g0sdn1_chatd-h3(4665)-1 12 21 unspecified role unspecified role prey prey in vitro In vitro 14 unspecified role unspecified role bait bait Region 651-944 Region 651-944 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain V5-tag V5-tag v5 tag v5 tag GKPIPNPLLGLDST epitope tag GKPIPNPLLGLDST epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction h3(120)-g0sdn1_chatd-1 13 22 unspecified role unspecified role bait bait Biotin-tag Biotin-tag biotin tag biotin tag n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 14 unspecified role unspecified role prey prey Region 651-944 Region 651-944 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction g0sdn1_chatd-g0shk5_chatd-1 1 14 unspecified role unspecified role unspecified role unspecified role Region 521-651 Region 521-651 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 18 unspecified role unspecified role unspecified role unspecified role Region 1-192 Region 1-192 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction g0sdn1_chatd-h4_xenla-2 3 17 unspecified role unspecified role prey prey ecolx Escherichia coli 15 unspecified role unspecified role prey prey ecolx Escherichia coli 14 unspecified role unspecified role bait bait Region 772-944 Region 772-944 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain V5-tag V5-tag v5 tag v5 tag GKPIPNPLLGLDST epitope tag GKPIPNPLLGLDST epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 1-447 Region 1-447 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli association association h3(4665)-g0sdn1_chatd-1 10 21 unspecified role unspecified role bait bait Biotin-tag Biotin-tag biotin tag biotin tag n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 14 unspecified role unspecified role prey prey Region 651-944 Region 651-944 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction g0sdn1_chatd-g0shk5_chatd-2 11 14 unspecified role unspecified role unspecified role unspecified role Region 521-651 Region 521-651 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 18 unspecified role unspecified role unspecified role unspecified role Region 1-192 Region 1-192 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction g0shk5_chatd-h4_xenla-1 7 18 unspecified role unspecified role bait bait Region 206-485 Region 206-485 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain V5-tag V5-tag v5 tag v5 tag GKPIPNPLLGLDST epitope tag GKPIPNPLLGLDST epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 17 unspecified role unspecified role prey prey ecolx Escherichia coli 15 unspecified role unspecified role prey prey ecolx Escherichia coli association association g0sdn1_chatd-pol1-1 6 16 unspecified role unspecified role prey prey TAP-tag TAP-tag tandem tag tandem tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 14 unspecified role unspecified role bait bait Region 521-651 Region 521-651 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain V5-tag V5-tag v5 tag v5 tag GKPIPNPLLGLDST epitope tag GKPIPNPLLGLDST epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association g0sdn1_chatd-h2b(2648)-1 4 20 unspecified role unspecified role unspecified role unspecified role in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Region 651-944 Region 651-944 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction