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      Relaxed Chromatin Formation and Weak Suppression of Homologous Pairing by the Testis-Specific Linker Histone H1T.

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          Abstract

          Linker histones bind to nucleosomes and compact polynucleosomes into a higher-order chromatin configuration. Somatic and germ cell-specific linker histone subtypes have been identified and may have distinct functions. In this study, we reconstituted polynucleosomes containing human histones H1.2 and H1T, as representative somatic and germ cell-specific linker histones, respectively, and found that H1T forms less compacted chromatin, as compared to H1.2. An in vitro homologous pairing assay revealed that H1T weakly inhibited RAD51/RAD54-mediated homologous pairing in chromatin, although the somatic H1 subtypes, H1.0, H1.1, H1.2, H1.3, H1.4, and H1.5, substantially suppressed it. An in vivo recombination assay revealed that H1T overproduction minimally affected the recombination frequency, but significant suppression was observed when H1.2 was overproduced in human cells. These results suggested that the testis-specific linker histone, H1T, possesses a specific function to produce the chromatin architecture required for proper chromosome regulation, such as homologous recombination.

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          Author and article information

          Journal
          Biochemistry
          Biochemistry
          American Chemical Society (ACS)
          1520-4995
          0006-2960
          Feb 02 2016
          : 55
          : 4
          Affiliations
          [1 ] Laboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University , 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.
          [2 ] Department of Cellular Biology, Research Institute for Radiation Biology and Medicine, Hiroshima University , 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8553, Japan.
          [3 ] Institute for Medical-oriented Structural Biology, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.
          Article
          10.1021/acs.biochem.5b01126
          26757249
          e639dea7-eca4-4da7-b614-45df142c8c8e
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