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PMID: 15282323 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Cluster analysis of mass spectrometry data reveals a novel component of SAGA.

Molecular and cellular biology ·Vol. 24 ·No. 16 ·2004-08-00 ·Pages 7249-59

Powell DW, Weaver CM, Jennings JL, McAfee KJ, He Y, Weil PA, Link AJ

Abstract

The SAGA histone acetyltransferase and TFIID complexes play key roles in eukaryotic transcription. Using hierarchical cluster analysis of mass spectrometry data to identify proteins that copurify with components of the budding yeast TFIID transcription complex, we discovered that an uncharacterized protein corresponding to the YPL047W open reading frame significantly associated with shared components of the TFIID and SAGA complexes. Using mass spectrometry and biochemical assays, we show that YPL047W (SGF11, 11-kDa SAGA-associated factor) is an integral subunit of SAGA. However, SGF11 does not appear to play a role in SAGA-mediated histone acetylation. DNA microarray analysis showed that SGF11 mediates transcription of a subset of SAGA-dependent genes, as well as SAGA-independent genes. SAGA purified from a sgf11 Delta deletion strain has reduced amounts of Ubp8p, and a ubp8 Delta deletion strain shows changes in transcription similar to those seen with the sgf11 Delta deletion strain. Together, these data show that Sgf11p is a novel component of the yeast SAGA complex and that SGF11 regulates transcription of a subset of SAGA-regulated genes. Our data suggest that the role of SGF11 in transcription is independent of SAGA's histone acetyltransferase activity but may involve Ubp8p recruitment to or stabilization in SAGA.

MeSH Terms
Acetyltransferases/chemistry,genetics,metabolism Cluster Analysis Gene Expression Regulation, Fungal Histone Acetyltransferases Mass Spectrometry Multienzyme Complexes Oligonucleotide Array Sequence Analysis Open Reading Frames Protein Subunits/chemistry,genetics,metabolism Saccharomyces cerevisiae/genetics,metabolism Saccharomyces cerevisiae Proteins/chemistry,genetics,metabolism Transcription Factor TFIID/chemistry,genetics,metabolism Transcription Factors/chemistry,genetics,metabolism Transcription, Genetic
Chemicals
Multienzyme Complexes Protein Subunits SGF11 protein, S cerevisiae Saccharomyces cerevisiae Proteins Transcription Factor TFIID Transcription Factors Acetyltransferases Histone Acetyltransferases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Powell David W
Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232-2363, USA.
Weaver Connie M
Jennings Jennifer L
McAfee K Jill
He Yue
Weil P Anthony
Link Andrew J
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/MCB.24.16.7249-7259.2004
Published
2004-08-00
Pages
7249-59
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC479721
Subset
IM
Grants
NCI NIH HHS · CA098131 · United States
NIGMS NIH HHS · R56 GM052461 · United States
NCI NIH HHS · 1 P50 CA90949 · United States
NHLBI NIH HHS · P01 HL068744 · United States
NCI NIH HHS · P50 CA098131 · United States
NIGMS NIH HHS · R01 GM052461 · United States
NCI NIH HHS · P50 CA090949 · United States
NHLBI NIH HHS · T32-HL69765 · United States
NIGMS NIH HHS · GM64779 · United States
NHLBI NIH HHS · T32 HL069765 · United States
NIGMS NIH HHS · R01 GM064779 · United States
NIGMS NIH HHS · R01 GM068900 · United States
NIEHS NIH HHS · ES11993 · United States
NINDS NIH HHS · R01 NS043952 · United States
NINDS NIH HHS · NS43952 · United States
NIGMS NIH HHS · GM52461 · United States
NHLBI NIH HHS · HL68744 · United States
NIEHS NIH HHS · R01 ES011993 · United States
External Links
PubMed source DOI: 10.1128/MCB.24.16.7249-7259.2004 PMC Full Text View journal details
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