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

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

doi:10.1038/383269a0

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

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

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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.

Original language	English (US)
Pages (from-to)	269-272
Number of pages	4
Journal	Nature
Volume	383
Issue number	6597
DOIs	https://doi.org/10.1038/383269a0
State	Published - 1996
Externally published	Yes

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title = "Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines",

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.",

author = "Kuo, {M. H.} and Brownell, {J. E.} and Sobel, {R. E.} and Ranalli, {T. A.} and Cook, {R. G.} and Edmondson, {D. G.} and Roth, {S. Y.} and Allis, {C. D.}",

year = "1996",

doi = "10.1038/383269a0",

language = "English (US)",

volume = "383",

pages = "269--272",

journal = "Nature",

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T1 - Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines

AU - Kuo, M. H.

AU - Brownell, J. E.

AU - Sobel, R. E.

AU - Ranalli, T. A.

AU - Cook, R. G.

AU - Edmondson, D. G.

AU - Roth, S. Y.

AU - Allis, C. D.

PY - 1996

Y1 - 1996

N2 - 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.

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

Abstract

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