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Curr Genet. 2018 Oct;64(5):1015-1019. doi: 10.1007/s00294-018-0825-9. Epub 2018 Mar 16.

The conserved histone variant H2A.Z illuminates meiotic recombination initiation.

Author information

1
Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Tokyo, 153-8902, Japan.
2
Memorial Sloan Kettering Cancer Center, New York, 10065, USA.
3
Kazusa DNA Research Institute, Chiba, 292-0818, Japan.
4
Advanced ICT Research Institute Kobe, National Institute of Information and Communications Technology, Kobe, 651-2492, Japan.
5
Graduate School of Frontier Biosciences, Osaka University, Suita, 565-0871, Japan.
6
Department of Biological Sciences, Faculty of Science and Engineering, Chuo University, Tokyo, 112-8551, Japan.
7
Department of Biological Sciences, Faculty of Science and Engineering, Chuo University, Tokyo, 112-8551, Japan. tyamada@bio.chuo-u.ac.jp.

Abstract

Meiotic recombination ensures faithful chromosome segregation and confers genetic diversity to gametes, and thus, is a key DNA-templated reaction not only for sexual reproduction, but also evolution. This recombination is initiated by programmed DNA double strand breaks (DSBs), which are mainly formed at recombination hotspots. As meiotic DSB formation requires multiple proteins, it is regulated by chromatin structure. In particular, DSB occurs in a higher-order chromatin architecture termed "axis-loop", in which many loops protrude from proteinaceous axis. Previous studies have suggested that assembly of this structure is dependent on chromatin binding of cohesin, which in turn recruits proteins implicated in DSB formation. However, roles of chromatin in meiotic DSB formation are not fully characterized. This review article summarizes our recent report showing that the conserved histone H2A variant H2A.Z promotes meiotic DSB formation in fission yeast. Through a series of experiments, we found that, in H2A.Z-lacking mutants, multiple proteins involved in DSB formation, but not cohesin subunits, are less associated with chromatin. Strikingly, nuclei were more compact in the absence of H2A.Z. These observations led us to propose that fission yeast H2A.Z promotes meiotic DSB formation partly through modulating chromosome architecture to enhance interaction between DSB-related proteins and cohesin-loaded chromatin. In addition, biological implications of our findings are discussed, and their relevance to DSB formation in other species as well as to other DNA-related events are also provided.

KEYWORDS:

Chromatin; DNA double strand break (DSB); Histone H2A.Z; Meiosis

PMID:
29549582
DOI:
10.1007/s00294-018-0825-9
[Indexed for MEDLINE]

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