{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Demeny MA"],"funding":["Worldwide Cancer Research"],"pagination":["e316"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1820849"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["2(3)"],"pubmed_abstract":["TFIID plays a role in nucleating RNA polymerase II preinitiation complex assembly on protein-coding genes. TFIID is a multisubunit complex comprised of the TATA box binding protein (TBP) and 14 TBP-associated factors (TAFs). Another class of multiprotein transcriptional regulatory complexes having histone acetyl transferase (HAT) activity, and containing TAFs, includes TFTC, STAGA and the PCAF/GCN5 complex. Looking for as yet undiscovered subunits by a proteomic approach, we had identified TAF8 and SPT7L in human TFTC preparations. Subsequently, however, we demonstrated that TAF8 was not a stable component of TFTC, but that it is present in a small TAF complex (SMAT), containing TAF8, TAF10 and SPT7L, that co-purified with TFTC. Thus, TAF8 is a subunit of both TFIID and SMAT. The latter ha"],"journal":["PloS one"],"pubmed_title":["Identification of a small TAF complex and its role in the assembly of TAF-containing complexes."],"pmcid":["PMC1820849"],"funding_grant_id":["03-084"],"pubmed_authors":["Kessler P","Argentini M","Richardot M","Demeny MA","Janoshazi A","Soutoglou E","Nagy Z","Scheer E","Tora L"],"additional_accession":[]},"is_claimable":false,"name":"Identification of a small TAF complex and its role in the assembly of TAF-containing complexes.","description":"TFIID plays a role in nucleating RNA polymerase II preinitiation complex assembly on protein-coding genes. TFIID is a multisubunit complex comprised of the TATA box binding protein (TBP) and 14 TBP-associated factors (TAFs). Another class of multiprotein transcriptional regulatory complexes having histone acetyl transferase (HAT) activity, and containing TAFs, includes TFTC, STAGA and the PCAF/GCN5 complex. Looking for as yet undiscovered subunits by a proteomic approach, we had identified TAF8 and SPT7L in human TFTC preparations. Subsequently, however, we demonstrated that TAF8 was not a stable component of TFTC, but that it is present in a small TAF complex (SMAT), containing TAF8, TAF10 and SPT7L, that co-purified with TFTC. Thus, TAF8 is a subunit of both TFIID and SMAT. The latter ha","dates":{"release":"2007-01-01T00:00:00Z","publication":"2007 Mar","modification":"2026-05-29T16:45:38.793Z","creation":"2019-03-26T23:02:18Z"},"accession":"S-EPMC1820849","cross_references":{"pubmed":["17375202"],"doi":["10.1371/journal.pone.0000316"]}}