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/ http://www.ebi.ac.uk/ gumbs-2003-1 High-affinity DNA binding by a Mot1p-TBP complex: implications for TAF-independent transcription. in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Gumbs OH., Campbell AM., Weil PA. Interaction involved 43 bp DNA duplex containing a consensus TATA box, TATAAAA. This was labeled with a rhodamine derivative. EMBO J. (0261-4189) 2003 IMEx Gumbs OH., Campbell AM., Weil PA., Gumbs OH., Campbell AM., Weil PA. Only protein-protein interactions imex curation imex curation tbp_yeast TATA-box-binding protein YER148W SPT15 BTF1 TBP1 TATA-box factor TATA-binding factor TATA sequence-binding protein Transcription factor D Transcription initiation factor TFIID TBP subunit protein protein yeast Saccharomyces cerevisiae Baker's yeast MADEERLKEFKEANKIVFDPNTRQVWENQNRDGTKPATTFQSEEDIKRAAPESEKDTSATSGIVPTLQNIVATVTLGCRLDLKTVALHARNAEYNPKRFAAVIMRIREPKTTALIFASGKMVVTGAKSEDDSKLASRKYARIIQKIGFAAKFTDFKIQNIVGSCDVKFPIRLEGLAFSHGTFSSYEPELFPGLIYRMVKPKIVLLIFVSGKIVLTGAKQREEIYQAFEAIYPVLSEFRKM 50365FFF1D3718CE mot1_yeast TATA-binding protein-associated factor MOT1 MOT1 YPL082C LPF4C Modifier of transcription 1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MTSRVSRLDRQVILIETGSTQVVRNMAADQMGDLAKQHPEDILSLLSRVYPFLLVKKWETRVTAARAVGGIVAHAPSWDPNESDLVGGTNEGSPLDNAQVKLEHEMKIKLEEATQNNQLNLLQEDHHLSSLSDWKLNEILKSGKVLLASSMNDYNVLGKADDNIRKQAKTDDIKQETSMLNASDKANENKSNANKKSARMLAMARRKKKMSAKNTPKHPVDITESSVSKTLLNGKNMTNSAASLATSPTSNQLNPKLEITEQADESKLMIESTVRPLLEQHEIVAGLVWQFQGIYELLLDNLMSENWEIRHGAALGLRELVKKHAYGVSRVKGNTREENNLRNSRSLEDLASRLLTVFALDRFGDYVYDTVVAPVRESVAQTLAALLIHLDSTLSIKIFNCLEQLVLQDPLQTGLPNKIWEATHGGLLGIRYFVSIKTNFLFAHGLLENVVRIVLYGLNQSDDDVQSVAASILTPITSEFVKLNNSTIEILVTTIWSLLARLDDDISSSVGSIMDLLAKLCDHQEVLDILKNKALEHPSEWSFKSLVPKLYPFLRHSISSVRRAVLNLLIAFLSIKDDSTKNWLNGKVFRLVFQNILLEQNPELLQLSFDVYVALLEHYKVKHTEKTLDHVFSKHLQPILHLLNTPVGEKGKNYAMESQYILKPSQHYQLHPEKKRSISETTTDSDIPIPKNNEHINIDAPMIAGDITLLGLDVILNTRIMGAKAFALTLSMFQDSTLQSFFTNVLVRCLELPFSTPRMLAGIIVSQFCSSWLQKHPEGEKLPSFVSEIFSPVMNKQLLNRDEFPVFRELVPSLKALRTQCQSLLATFVDVGMLPQYKLPNVAIVVQGETEAGPHAFGVETAEKVYGEYYDKMFKSMNNSYKLLAKKPLEDSKHRVLMAINSAKESAKLRTGSILANYASSILLFDGLPLKLNPIIRSLMDSVKEERNEKLQTMAGESVVHLIQQLLENNKVNVSGKIVKNLCGFLCVDTSEVPDFSVNAEYKEKILTLIKESNSIAAQDDINLAKMSEEAQLKRKGGLITLKILFEVLGPSILQKLPQLRSILFDSLSDHENEEASKVDNEQGQKIVDSFGVLRALFPFMSDSLRSSEVFTRFPVLLTFLRSNLSVFRYSAARTFADLAKISSVEVMAYTIREILPLMNSAGSLSDRQGSTELIYHLSLSMETDVLPYVIFLIVPLLGRMSDSNEDVRNLATTTFASIIKLVPLEAGIADPKGLPEELVASRERERDFIQQMMDPSKAKPFKLPIAIKATLRKYQQDGVNWLAFLNKYHLHGILCDDMGLGKTLQTICIIASDQYLRKEDYEKTRSVESRALPSLIICPPSLTGHWENEFDQYAPFLKVVVYAGGPTVRLTLRPQLSDADIIVTSYDVARNDLAVLNKTEYNYCVLDEGHIIKNSQSKLAKAVKEITANHRLILTGTPIQNNVLELWSLFDFLMPGFLGTEKMFQERFAKPIAASRNSKTSSKEQEAGVLALEALHKQVLPFMLRRLKEDVLSDLPPKIIQDYYCELGDLQKQLYMDFTKKQKNVVEKDIENSEIADGKQHIFQALQYMRKLCNHPALVLSPNHPQLAQVQDYLKQTGLDLHDIINAPKLSALRTLLFECGIGEEDIDKKASQDQNFPIQNVISQHRALIFCQLKDMLDMVENDLFKKYMPSVTYMRLDGSIDPRDRQKVVRKFNEDPSIDCLLLTTKVGGLGLNLTGADTVIFVEHDWNPMNDLQAMDRAHRIGQKKVVNVYRIITKGTLEEKIMGLQKFKMNIASTVVNQQNSGLASMDTHQLLDLFDPDNVTSQDNEEKNNGDSQAAKGMEDIANETGLTGKAKEALGELKELWDPSQYEEEYNLDTFIKTLR 1A00005148D5632B spt15-mot1-4 mot1-TBP-TATA box ternary complex formation 134169 N/A 134170 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 134171 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) physical association physical association false false false 134169 Fig. 5 Purified TBP was bound to a TATA box sequence, then purified Mot1 was added. Addition of saturating levels of ATP induced complex dissociation. Evidence presented in this paper that dissociation requires Mot1 ATPase activity. Evidence presented in this paper that Mot1 binds directly to TBP in an ATP dependent manner. Affinity constant (Kd,app) of the TBP-Mot1 interaction is 1x10-9M.