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. 1996 Sep 19;383(6597):269-72.
doi: 10.1038/383269a0.

Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines

M H Kuo  1 , J E Brownell, R E Sobel, T A Ranalli, R G Cook, D G Edmondson, S Y Roth, C D Allis
Affiliations

Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines

M H Kuo et al. Nature. .

Abstract

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.

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