Work

Structural Characterization of the Histone Variant macroH2A

Year: 2005

Type: article

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.

Source: Molecular and Cellular Biology

DOI: 10.1128/mcb.25.17.7616-7624.2005

Authors: Srinivas Chakravarthy, Sampath Kumar Y. Gundimella, Cecile Caron, Pierre-Yves Perche, John R. Pehrson, Saadi Khochbin, Karolin Luger

Institutions: Colorado State University, Inserm, Institut pour l'avancée des biosciences, University of Pennsylvania

Language: English

Topic: Genomics and Chromatin Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: March of Dimes Foundation, National Institutes of Health

OpenAlex ID: W2157569563

FWCI: 3.11

Cites: 34

Cited by: 183

Related to: 10