Current Genetics

, Volume 64, Issue 5, pp 1015–1019 | Cite as

The conserved histone variant H2A.Z illuminates meiotic recombination initiation

  • Shintaro Yamada
  • Kazuto Kugou
  • Da-Qiao Ding
  • Yurika Fujita
  • Yasushi Hiraoka
  • Hiroshi Murakami
  • Kunihiro Ohta
  • Takatomi YamadaEmail author


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.


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



We regret that much of the relevant work could not be cited due to space limitations.


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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  • Shintaro Yamada
    • 1
    • 5
  • Kazuto Kugou
    • 1
    • 6
  • Da-Qiao Ding
    • 3
  • Yurika Fujita
    • 1
  • Yasushi Hiraoka
    • 3
    • 4
  • Hiroshi Murakami
    • 2
  • Kunihiro Ohta
    • 1
  • Takatomi Yamada
    • 2
    Email author
  1. 1.Department of Life Sciences, Graduate School of Arts and SciencesThe University of TokyoTokyoJapan
  2. 2.Department of Biological Sciences, Faculty of Science and EngineeringChuo UniversityTokyoJapan
  3. 3.Advanced ICT Research Institute Kobe, National Institute of Information and Communications TechnologyKobeJapan
  4. 4.Graduate School of Frontier BiosciencesOsaka UniversitySuitaJapan
  5. 5.Memorial Sloan Kettering Cancer CenterNew YorkUSA
  6. 6.Kazusa DNA Research InstituteChibaJapan

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