Histone H2A.Z cooperates with RNAi and heterochromatin factors to suppress antisense RNAs

Martin Zofall, Tamás Fischer, Ke Zhang, Ming Zhou, Bowen Cui, Timothy D. Veenstra and Shiv I. S. Grewal ()
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Martin Zofall: Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health Bethesda
Tamás Fischer: Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health Bethesda
Ke Zhang: Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health Bethesda
Ming Zhou: Laboratory of Proteomics and Analytical Technologies, Advanced Technology Program, SAIC-Frederick, Inc., NCI-Frederick, Frederick, Maryland 21702, USA
Bowen Cui: Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health Bethesda
Timothy D. Veenstra: Laboratory of Proteomics and Analytical Technologies, Advanced Technology Program, SAIC-Frederick, Inc., NCI-Frederick, Frederick, Maryland 21702, USA
Shiv I. S. Grewal: Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health Bethesda

Nature, 2009, vol. 461, issue 7262, 419-422

Abstract: Antisense RNAs suppressed by histone H2A.Z Unregulated transcription of antisense RNAs is potentially deleterious to a cell because sense–antisense pairing could affect gene expression. In this study, Zofall et al. examine how antisense transcription is held in check in fission yeast. They find that the variant histone H2A.Z, which localizes to the 5′ ends of genes, cooperates with heterochromatin and RNA interference factors to mediate suppression of antisense transcription.

Date: 2009
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DOI: 10.1038/nature08321

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