Abstract
Acetylation of histone H3 lysine 56 (H3-K56) occurs in S phase, and cells lacking H3-K56 acetylation are sensitive to DNA-damaging agents. However, the histone acetyltransferase (HAT) that catalyzes global H3-K56 acetylation has not been found. Here we show that regulation of Ty1 transposition gene product 109 (Rtt109) is an H3-K56 HAT. Cells lacking Rtt109 or expressing rtt109 mutants with alterations at a conserved aspartate residue lose H3-K56 acetylation and exhibit increased sensitivity toward genotoxic agents, as well as elevated levels of spontaneous chromosome breaks. Thus, Rtt109, which shares no sequence homology with any other known HATs, is a unique HAT that acetylates H3-K56.
Publication types
-
Research Support, N.I.H., Extramural
MeSH terms
-
Acetylation
-
Amino Acid Sequence
-
Camptothecin / pharmacology
-
Catalytic Domain
-
Chromosome Breakage
-
DNA Damage
-
DNA Replication*
-
Histone Acetyltransferases / chemistry
-
Histone Acetyltransferases / genetics
-
Histone Acetyltransferases / metabolism*
-
Histones / metabolism*
-
Hydroxyurea / pharmacology
-
Lysine / metabolism*
-
Methyl Methanesulfonate / pharmacology
-
Molecular Sequence Data
-
Mutagenesis, Site-Directed
-
Mutagens / pharmacology
-
Mutation
-
Recombinant Proteins / metabolism
-
S Phase
-
Saccharomyces cerevisiae / genetics
-
Saccharomyces cerevisiae / metabolism*
-
Saccharomyces cerevisiae Proteins / chemistry
-
Saccharomyces cerevisiae Proteins / genetics
-
Saccharomyces cerevisiae Proteins / metabolism*
-
Sequence Homology, Amino Acid
Substances
-
Histones
-
Mutagens
-
Recombinant Proteins
-
Saccharomyces cerevisiae Proteins
-
Methyl Methanesulfonate
-
Histone Acetyltransferases
-
Rtt109 protein, S cerevisiae
-
Lysine
-
Hydroxyurea
-
Camptothecin