Affiliation:
1. Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794-5215
Abstract
Abstract
The N-terminal alanine residues of the silencing protein Sir3 and of Orc1 are acetylated by the NatA Nα-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.
Publisher
Oxford University Press (OUP)
Cited by
68 articles.
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