Acetylation in histone H3 globular domain regulates gene expression in yeast

Feng Xu, Kangling Zhang, Michael Grunstein

Research output: Contribution to journalArticle

286 Citations (Scopus)

Abstract

In Saccharomyces cerevisiae, known histone acetylation sites regulating gene activity are located in the N-terminal tails protruding from the nucleosome core. We report lysine 56 in histone H3 as a novel acetylation site that is located in the globular domain, where it extends toward the DNA major groove at the entry-exit points of the DNA superhelix as it wraps around the nucleosome. We show that K56 acetylation is enriched preferentially at certain active genes, such as those coding for histones. SPT10, a putative acetyltransferase, is required for cell cycle-specific K56 acetylation at histone genes. This allows recruitment of the nucleosome remodeling factor Snf5 and subsequent transcription. These findings indicate that histone H3 K56 acetylation at the entry-exit gate enables recruitment of the SWI/SNF nucleosome remodeling complex and so regulates gene activity.

Original languageEnglish (US)
Pages (from-to)375-385
Number of pages11
JournalCell
Volume121
Issue number3
DOIs
StatePublished - May 6 2005
Externally publishedYes

Fingerprint

Acetylation
Gene expression
Histones
Yeast
Nucleosomes
Yeasts
Gene Expression
Genes
Acetyltransferases
DNA
Transcription
Lysine
Saccharomyces cerevisiae
Cell Cycle
Cells

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Acetylation in histone H3 globular domain regulates gene expression in yeast. / Xu, Feng; Zhang, Kangling; Grunstein, Michael.

In: Cell, Vol. 121, No. 3, 06.05.2005, p. 375-385.

Research output: Contribution to journalArticle

Xu, Feng ; Zhang, Kangling ; Grunstein, Michael. / Acetylation in histone H3 globular domain regulates gene expression in yeast. In: Cell. 2005 ; Vol. 121, No. 3. pp. 375-385.
@article{7701b040cee446398e6cc8e4d9a360c2,
title = "Acetylation in histone H3 globular domain regulates gene expression in yeast",
abstract = "In Saccharomyces cerevisiae, known histone acetylation sites regulating gene activity are located in the N-terminal tails protruding from the nucleosome core. We report lysine 56 in histone H3 as a novel acetylation site that is located in the globular domain, where it extends toward the DNA major groove at the entry-exit points of the DNA superhelix as it wraps around the nucleosome. We show that K56 acetylation is enriched preferentially at certain active genes, such as those coding for histones. SPT10, a putative acetyltransferase, is required for cell cycle-specific K56 acetylation at histone genes. This allows recruitment of the nucleosome remodeling factor Snf5 and subsequent transcription. These findings indicate that histone H3 K56 acetylation at the entry-exit gate enables recruitment of the SWI/SNF nucleosome remodeling complex and so regulates gene activity.",
author = "Feng Xu and Kangling Zhang and Michael Grunstein",
year = "2005",
month = "5",
day = "6",
doi = "10.1016/j.cell.2005.03.011",
language = "English (US)",
volume = "121",
pages = "375--385",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "3",

}

TY - JOUR

T1 - Acetylation in histone H3 globular domain regulates gene expression in yeast

AU - Xu, Feng

AU - Zhang, Kangling

AU - Grunstein, Michael

PY - 2005/5/6

Y1 - 2005/5/6

N2 - In Saccharomyces cerevisiae, known histone acetylation sites regulating gene activity are located in the N-terminal tails protruding from the nucleosome core. We report lysine 56 in histone H3 as a novel acetylation site that is located in the globular domain, where it extends toward the DNA major groove at the entry-exit points of the DNA superhelix as it wraps around the nucleosome. We show that K56 acetylation is enriched preferentially at certain active genes, such as those coding for histones. SPT10, a putative acetyltransferase, is required for cell cycle-specific K56 acetylation at histone genes. This allows recruitment of the nucleosome remodeling factor Snf5 and subsequent transcription. These findings indicate that histone H3 K56 acetylation at the entry-exit gate enables recruitment of the SWI/SNF nucleosome remodeling complex and so regulates gene activity.

AB - In Saccharomyces cerevisiae, known histone acetylation sites regulating gene activity are located in the N-terminal tails protruding from the nucleosome core. We report lysine 56 in histone H3 as a novel acetylation site that is located in the globular domain, where it extends toward the DNA major groove at the entry-exit points of the DNA superhelix as it wraps around the nucleosome. We show that K56 acetylation is enriched preferentially at certain active genes, such as those coding for histones. SPT10, a putative acetyltransferase, is required for cell cycle-specific K56 acetylation at histone genes. This allows recruitment of the nucleosome remodeling factor Snf5 and subsequent transcription. These findings indicate that histone H3 K56 acetylation at the entry-exit gate enables recruitment of the SWI/SNF nucleosome remodeling complex and so regulates gene activity.

UR - http://www.scopus.com/inward/record.url?scp=18844413266&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=18844413266&partnerID=8YFLogxK

U2 - 10.1016/j.cell.2005.03.011

DO - 10.1016/j.cell.2005.03.011

M3 - Article

VL - 121

SP - 375

EP - 385

JO - Cell

JF - Cell

SN - 0092-8674

IS - 3

ER -