Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines.
The yeast transcriptional adaptor, Gcn5p, is a catalytic subunit of a nuclear (type A) histone acetyltransferase linking histone acetylation to gene activation. Here we report that Gcn5p acetylates histones H3 and H4 non-randomly at specific lysines in the amino-terminal domains. Lysine 14 of H3 and lysines 8 and 16 of ... H4 are highly preferred acetylation sites for Gcn5p. We also demonstrate that lysine 9 is the preferred position of acetylation in newly synthesized yeast H3 in vivo. This finding, along with the fact that lysines 5 and 12 in H4 are predominant acetylation sites during chromatin assembly of many organisms, indicates that Gcn5p acetylates a distinct set of lysines that do not overlap with those sites characteristically used by type B histone acetyltransferases for histone deposition and chromatin assembly.
Mesh Terms:
Acetylation, Acetyltransferases, Amino Acid Sequence, Animals, Cattle, Chickens, DNA-Binding Proteins, Fungal Proteins, Histone Acetyltransferases, Histones, Lysine, Molecular Sequence Data, Protein Kinases, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Substrate Specificity, Tetrahymena thermophila, Transcription, Genetic
Acetylation, Acetyltransferases, Amino Acid Sequence, Animals, Cattle, Chickens, DNA-Binding Proteins, Fungal Proteins, Histone Acetyltransferases, Histones, Lysine, Molecular Sequence Data, Protein Kinases, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Substrate Specificity, Tetrahymena thermophila, Transcription, Genetic
Nature
Date: Sep. 19, 1996
PubMed ID: 8805705
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