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PMID: 16107708 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Structural characterization of the histone variant macroH2A.

Molecular and cellular biology ·Vol. 25 ·No. 17 ·2005-09-00 ·Pages 7616-24

Chakravarthy S, Gundimella SK, Caron C, Perche PY, Pehrson JR, Khochbin S, Luger K

Abstract

macroH2A is an H2A variant with a highly unusual structural organization. It has a C-terminal domain connected to the N-terminal histone domain by a linker. Crystallographic and biochemical studies show that changes in the L1 loop in the histone fold region of macroH2A impact the structure and potentially the function of nucleosomes. The 1.6-A X-ray structure of the nonhistone region reveals an alpha/beta fold which has previously been found in a functionally diverse group of proteins. This region associates with histone deacetylases and affects the acetylation status of nucleosomes containing macroH2A. Thus, the unusual domain structure of macroH2A integrates independent functions that are instrumental in establishing a structurally and functionally unique chromatin domain.

MeSH Terms
Acetylation Amino Acid Sequence Animals Cell Line Chlorocebus aethiops Chromatin/metabolism Crystallography, X-Ray Histones/chemistry,metabolism Humans Mice Models, Molecular Molecular Sequence Data Protein Structure, Tertiary Sequence Alignment Xenopus laevis
Chemicals
Chromatin Histones macroH2A histone
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Chakravarthy Srinivas
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, 80523-1870, USA.
Gundimella Sampath Kumar Y
Caron Cecile
Perche Pierre-Yves
Pehrson John R
Khochbin Saadi
Luger Karolin
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/MCB.25.17.7616-7624.2005
Published
2005-09-00
Pages
7616-24
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC1190287
Subset
IM
External Links
PubMed source DOI: 10.1128/MCB.25.17.7616-7624.2005 PMC Full Text View journal details
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