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PMID: 15454564 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Importance of the Sir3 N terminus and its acetylation for yeast transcriptional silencing.

Genetics ·Vol. 168 ·No. 1 ·2004-09-00 ·Pages 547-51

Wang X, Connelly JJ, Wang CL, Sternglanz R

Abstract

The N-terminal alanine residues of the silencing protein Sir3 and of Orc1 are acetylated by the NatA Nalpha-acetyltransferase. Mutations demonstrate that the N terminus of Sir3 is important for its function. Sir3 and, perhaps, also Orc1 are the NatA substrates whose lack of acetylation in ard1 and nat1 mutants explains the silencing defect of those mutants.

MeSH Terms
Acetylation Acetyltransferases/genetics Alanine/metabolism DNA-Binding Proteins/genetics,metabolism Gene Expression Regulation, Fungal Mutation/genetics N-Terminal Acetyltransferase A Origin Recognition Complex Saccharomyces cerevisiae/genetics Saccharomyces cerevisiae Proteins Silencer Elements, Transcriptional/genetics Silent Information Regulator Proteins, Saccharomyces cerevisiae/genetics,metabolism Species Specificity
Chemicals
DNA-Binding Proteins NAT1 protein, S cerevisiae ORC1 protein, S cerevisiae Origin Recognition Complex SIR3 protein, S cerevisiae Saccharomyces cerevisiae Proteins Silent Information Regulator Proteins, Saccharomyces cerevisiae Acetyltransferases protein N-terminal acetyltransferase N-Terminal Acetyltransferase A ARD1 protein, S cerevisiae Alanine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Wang Xiaorong
Department of Biochemistry and Cell Biology, Stony Brook University, New York 11794-5215, USA.
Connelly Jessica J
Wang Chia-Lin
Sternglanz Rolf
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Article Info
Journal
Genetics
Abbr.
Genetics
ISSN
0016-6731
DOI
10.1534/genetics.104.028803
Published
2004-09-00
Pages
547-51
Language
English
Region
United States
NLM ID
0374636
PMCID
PMC1448112
Subset
IM
Grants
NIGMS NIH HHS · R01 GM028220 · United States
NIGMS NIH HHS · R56 GM028220 · United States
NIGMS NIH HHS · GM-28220 · United States
External Links
PubMed source DOI: 10.1534/genetics.104.028803 PMC Full Text View journal details
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