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PMID: 15657441 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

H2B ubiquitin protease Ubp8 and Sgf11 constitute a discrete functional module within the Saccharomyces cerevisiae SAGA complex.

Molecular and cellular biology ·Vol. 25 ·No. 3 ·2005-02-00 ·Pages 1162-72

Ingvarsdottir K, Krogan NJ, Emre NC, Wyce A, Thompson NJ, Emili A, Hughes TR, Greenblatt JF, Berger SL

Abstract

The SAGA complex is a multisubunit protein complex involved in transcriptional regulation in Saccharomyces cerevisiae. SAGA combines proteins involved in interactions with DNA-bound activators and TATA-binding protein (TBP), as well as enzymes for histone acetylation (Gcn5) and histone deubiquitylation (Ubp8). We recently showed that H2B ubiquitylation and Ubp8-mediated deubiquitylation are both required for transcriptional activation. For this study, we investigated the interaction of Ubp8 with SAGA. Using mutagenesis, we identified a putative zinc (Zn) binding domain within Ubp8 as being critical for the association with SAGA. The Zn binding domain is required for H2B deubiquitylation and for growth on media requiring Ubp8's function in gene activation. Furthermore, we identified an 11-kDa subunit of SAGA, Sgf11, and showed that it is required for the Ubp8 association with SAGA and for H2B deubiquitylation. Different approaches indicated that the functions of Ubp8 and Sgf11 are related and separable from those of other components of SAGA. In particular, the profiles of Ubp8 and Sgf11 deletions were remarkably similar in microarray analyses and synthetic genetic interactions and were distinct from those of the Spt3 and Spt8 subunits of SAGA, which are involved in TBP regulation. These data indicate that Ubp8 and Sgf11 likely represent a new functional module within SAGA that is involved in gene regulation through H2B deubiquitylation.

MeSH Terms
Amino Acid Sequence DNA-Binding Proteins/metabolism Gene Expression Regulation, Fungal/physiology Histone Acetyltransferases Histones/metabolism Microarray Analysis Molecular Sequence Data Mutation/genetics Protein Kinases/metabolism Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins/metabolism Transcription Factors/metabolism Transcriptional Activation Ubiquitin/metabolism Zinc/metabolism
Chemicals
DNA-Binding Proteins Histones SGF11 protein, S cerevisiae Saccharomyces cerevisiae Proteins Transcription Factors Ubiquitin GCN5 protein, S cerevisiae Histone Acetyltransferases Protein Kinases Zinc
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Ingvarsdottir Kristin
The Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA.
Krogan Nevan J
Emre N C Tolga
Wyce Anastasia
Thompson Natalie J
Emili Andrew
Hughes Timothy R
Greenblatt Jack F
Berger Shelley L
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
2005-02-00
Pages
1162-72
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC544016
Subset
IM
Grants
NIGMS NIH HHS · R01 GM055360 · United States
NIGMS NIH HHS · T32 GM008216 · United States
NIGMS NIH HHS · GM 55360 · United States
NIGMS NIH HHS · T32 GM 008216 · United States
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