Histone acetyltransferase complexes: one size doesn't fit all

Over the past 10 years, the study of histone acetyltransferases (HATs) has advanced significantly, and a number of HATs have been isolated from various organisms. It emerged that HATs are highly diverse and generally contain multiple subunits. The functions of the catalytic subunit depend largely on...

Full description

Saved in:
Bibliographic Details
Published inNature reviews. Molecular cell biology Vol. 8; no. 4; pp. 284 - 295
Main Authors Workman, Jerry L, Lee, Kenneth K
Format Journal Article
LanguageEnglish
Published England Nature Publishing Group 01.04.2007
Subjects
Animals
Chromatin - metabolism
Deoxyribonucleic acid
DNA
DNA methylation
DNA Repair
Enzymes
Epigenetics
Genetic aspects
Genetic regulation
Histone Acetyltransferases - chemistry
Histone Acetyltransferases - metabolism
Histones
Histones - metabolism
Humans
Models, Molecular
Physiological aspects
Protein Structure, Tertiary
Proteins
Substrate Specificity
Transferases
Yeast
United States
Online AccessGet full text

Cover

More Information
Summary:Over the past 10 years, the study of histone acetyltransferases (HATs) has advanced significantly, and a number of HATs have been isolated from various organisms. It emerged that HATs are highly diverse and generally contain multiple subunits. The functions of the catalytic subunit depend largely on the context of the other subunits in the complex. We are just beginning to understand the specialized roles of HAT complexes in chromosome decondensation, DNA-damage repair and the modification of non-histone substrates, as well as their role in the broader epigenetic landscape, including the role of protein domains within HAT complexes and the dynamic interplay between HAT complexes and existing histone modifications.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ISSN:1471-0072
1471-0080
DOI:10.1038/nrm2145