<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Demeny MA</submitter><funding>Worldwide Cancer Research</funding><pagination>e316</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC1820849</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>2(3)</volume><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</pubmed_abstract><journal>PloS one</journal><pubmed_title>Identification of a small TAF complex and its role in the assembly of TAF-containing complexes.</pubmed_title><pmcid>PMC1820849</pmcid><funding_grant_id>03-084</funding_grant_id><pubmed_authors>Kessler P</pubmed_authors><pubmed_authors>Argentini M</pubmed_authors><pubmed_authors>Richardot M</pubmed_authors><pubmed_authors>Demeny MA</pubmed_authors><pubmed_authors>Janoshazi A</pubmed_authors><pubmed_authors>Soutoglou E</pubmed_authors><pubmed_authors>Nagy Z</pubmed_authors><pubmed_authors>Scheer E</pubmed_authors><pubmed_authors>Tora L</pubmed_authors></additional><is_claimable>false</is_claimable><name>Identification of a small TAF complex and its role in the assembly of TAF-containing complexes.</name><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</description><dates><release>2007-01-01T00:00:00Z</release><publication>2007 Mar</publication><modification>2026-05-29T16:45:38.793Z</modification><creation>2019-03-26T23:02:18Z</creation></dates><accession>S-EPMC1820849</accession><cross_references><pubmed>17375202</pubmed><doi>10.1371/journal.pone.0000316</doi></cross_references></HashMap>