A Role for Gcn5 in Replication-Coupled Nucleosome Assembly

Rebecca J. Burgess, Hui Zhou, Junhong Han, Zhiguo Zhang

Research output: Contribution to journalArticle

101 Citations (Scopus)

Abstract

Acetylation of lysine residues at the H3 N terminus is proposed to function in replication-coupled (RC) nucleosome assembly, a process critical for the inheritance of epigenetic information and maintenance of genome stability. However, the role of H3 N-terminal lysine acetylation and the corresponding lysine acetyltransferase (KAT) in RC nucleosome assembly are not known. Here we show that Gcn5, a KAT that functions in transcription, works in parallel with Rtt109, the H3 lysine 56 KAT, to promote RC nucleosome assembly. Cells lacking both Gcn5 and Rtt109 are highly sensitive to DNA damaging agents. Moreover, cells lacking GCN5 or those that express N-terminal H3 mutants are compromised for deposition of new H3 onto replicating DNA and also show reduced binding of H3 to CAF-1, a histone chaperone involved in RC nucleosome assembly. These results demonstrate that Gcn5 regulates RC nucleosome assembly, in part, by promoting H3 association with CAF-1 via H3 acetylation.

Original languageEnglish (US)
Pages (from-to)469-480
Number of pages12
JournalMolecular Cell
Volume37
Issue number4
DOIs
StatePublished - Feb 26 2010

Fingerprint

Nucleosomes
Acetylation
Lysine
Histone Chaperones
Genomic Instability
DNA
Epigenomics
Maintenance

Keywords

  • DNA
  • PROTEINS

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

A Role for Gcn5 in Replication-Coupled Nucleosome Assembly. / Burgess, Rebecca J.; Zhou, Hui; Han, Junhong; Zhang, Zhiguo.

In: Molecular Cell, Vol. 37, No. 4, 26.02.2010, p. 469-480.

Research output: Contribution to journalArticle

Burgess, RJ, Zhou, H, Han, J & Zhang, Z 2010, 'A Role for Gcn5 in Replication-Coupled Nucleosome Assembly', Molecular Cell, vol. 37, no. 4, pp. 469-480. https://doi.org/10.1016/j.molcel.2010.01.020
Burgess, Rebecca J. ; Zhou, Hui ; Han, Junhong ; Zhang, Zhiguo. / A Role for Gcn5 in Replication-Coupled Nucleosome Assembly. In: Molecular Cell. 2010 ; Vol. 37, No. 4. pp. 469-480.
@article{122712e289d44fa698902728afff6ee9,
title = "A Role for Gcn5 in Replication-Coupled Nucleosome Assembly",
abstract = "Acetylation of lysine residues at the H3 N terminus is proposed to function in replication-coupled (RC) nucleosome assembly, a process critical for the inheritance of epigenetic information and maintenance of genome stability. However, the role of H3 N-terminal lysine acetylation and the corresponding lysine acetyltransferase (KAT) in RC nucleosome assembly are not known. Here we show that Gcn5, a KAT that functions in transcription, works in parallel with Rtt109, the H3 lysine 56 KAT, to promote RC nucleosome assembly. Cells lacking both Gcn5 and Rtt109 are highly sensitive to DNA damaging agents. Moreover, cells lacking GCN5 or those that express N-terminal H3 mutants are compromised for deposition of new H3 onto replicating DNA and also show reduced binding of H3 to CAF-1, a histone chaperone involved in RC nucleosome assembly. These results demonstrate that Gcn5 regulates RC nucleosome assembly, in part, by promoting H3 association with CAF-1 via H3 acetylation.",
keywords = "DNA, PROTEINS",
author = "Burgess, {Rebecca J.} and Hui Zhou and Junhong Han and Zhiguo Zhang",
year = "2010",
month = "2",
day = "26",
doi = "10.1016/j.molcel.2010.01.020",
language = "English (US)",
volume = "37",
pages = "469--480",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "4",

}

TY - JOUR

T1 - A Role for Gcn5 in Replication-Coupled Nucleosome Assembly

AU - Burgess, Rebecca J.

AU - Zhou, Hui

AU - Han, Junhong

AU - Zhang, Zhiguo

PY - 2010/2/26

Y1 - 2010/2/26

N2 - Acetylation of lysine residues at the H3 N terminus is proposed to function in replication-coupled (RC) nucleosome assembly, a process critical for the inheritance of epigenetic information and maintenance of genome stability. However, the role of H3 N-terminal lysine acetylation and the corresponding lysine acetyltransferase (KAT) in RC nucleosome assembly are not known. Here we show that Gcn5, a KAT that functions in transcription, works in parallel with Rtt109, the H3 lysine 56 KAT, to promote RC nucleosome assembly. Cells lacking both Gcn5 and Rtt109 are highly sensitive to DNA damaging agents. Moreover, cells lacking GCN5 or those that express N-terminal H3 mutants are compromised for deposition of new H3 onto replicating DNA and also show reduced binding of H3 to CAF-1, a histone chaperone involved in RC nucleosome assembly. These results demonstrate that Gcn5 regulates RC nucleosome assembly, in part, by promoting H3 association with CAF-1 via H3 acetylation.

AB - Acetylation of lysine residues at the H3 N terminus is proposed to function in replication-coupled (RC) nucleosome assembly, a process critical for the inheritance of epigenetic information and maintenance of genome stability. However, the role of H3 N-terminal lysine acetylation and the corresponding lysine acetyltransferase (KAT) in RC nucleosome assembly are not known. Here we show that Gcn5, a KAT that functions in transcription, works in parallel with Rtt109, the H3 lysine 56 KAT, to promote RC nucleosome assembly. Cells lacking both Gcn5 and Rtt109 are highly sensitive to DNA damaging agents. Moreover, cells lacking GCN5 or those that express N-terminal H3 mutants are compromised for deposition of new H3 onto replicating DNA and also show reduced binding of H3 to CAF-1, a histone chaperone involved in RC nucleosome assembly. These results demonstrate that Gcn5 regulates RC nucleosome assembly, in part, by promoting H3 association with CAF-1 via H3 acetylation.

KW - DNA

KW - PROTEINS

UR - http://www.scopus.com/inward/record.url?scp=76849084692&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=76849084692&partnerID=8YFLogxK

U2 - 10.1016/j.molcel.2010.01.020

DO - 10.1016/j.molcel.2010.01.020

M3 - Article

VL - 37

SP - 469

EP - 480

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 4

ER -