Journal
GENES & DEVELOPMENT
Volume 26, Issue 5, Pages 433-438Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.179416.111
Keywords
macroH2A; histone variant; ATRX; alpha-globin; chromatin remodeling; histone chaperone
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Funding
- NCI [T32-CA078207]
- NIH MSTP [T32-GM007280]
- Major State Basic Research Development Program, China [2011CB965300]
- National Natural Science Foundation of China [60905013, 60934004, 91019016]
- DFG [SFB TR5, SCHE1596/2-1]
- CIPSM
- NIH [DP2OD007447]
- Ellison Medical Foundation
- NCI/NIH [R01CA154683]
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The histone variant macroH2A generally associates with transcriptionally inert chromatin; however, the factors that regulate its chromatin incorporation remain elusive. Here, we identify the SWI/SNF helicase ATRX (alpha-thalassemia/MR, X-linked) as a novel macroH2A-interacting protein. Unlike its role in assisting H3.3 chromatin deposition, ATRX acts as a negative regulator of macroH2A's chromatin association. In human erythroleukemic cells deficient for ATRX, macroH2A accumulates at the HBA gene cluster on the subtelomere of chromosome 16, coinciding with the loss of alpha-globin expression. Collectively, our results implicate deregulation of macroH2A's distribution as a contributing factor to the alpha-thalassemia phenotype of ATRX syndrome.
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