γH2AX and its role in DNA double-strand break repairThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process.

Author:

Fillingham Jeffrey123,Keogh Michael-Christopher123,Krogan Nevan J.123

Affiliation:

1. Banting and Best Dept of Medical Research, University of Toronto, Toronto, ON M5S 1A8, Canada.

2. Dept of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02138, USA.

3. Dept of Cellular and Molecular Pharmacology, UCSF, San Francisco, CA 94143, USA.

Abstract

One of the earliest responses to a DNA double-strand break (DSB) is the carboxy-terminal phosphorylation of budding yeast H2A (metazoan histone H2AX) to create γH2A (or γΗ2ΑX). This chromatin modification stretches more than tens of kilobases around the DSB and has been proposed to play numerous roles in break recognition and repair, although it may not be the primary signal for many of these events. Studies suggest that γH2A(X) has 2 more direct roles: (i) to recruit cohesin around the DSB, and (ii) to maintain a checkpoint arrest. Recent work has identified other factors, including chromatin remodelers and protein phosphatases, which target γH2A(X) and regulate DSB repair/recovery.

Publisher

Canadian Science Publishing

Subject

Cell Biology,Molecular Biology,Biochemistry

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