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Structure of human nucleosome containing the testis-specific histone variant TSH2B.

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Urahama T, Horikoshi N, Osakabe A, Tachiwana H, Kurumizaka H
OpenAccess logo Acta Crystallogr F Struct Biol Commun 70 444-9 (2014)
Cited: 12 times
EuropePMC logo PMID: 24699735

Abstract

The human histone H2B variant TSH2B is highly expressed in testis and may function in the chromatin transition during spermatogenesis. In the present study, the crystal structure of the human testis-specific nucleosome containing TSH2B was determined at 2.8 Å resolution. A local structural difference between TSH2B and canonical H2B in nucleosomes was detected around the TSH2B-specific amino-acid residue Ser85. The TSH2B Ser85 residue does not interact with H4 in the nucleosome, but in the canonical nucleosome the H2B Asn84 residue (corresponding to the TSH2B Ser85 residue) forms water-mediated hydrogen bonds with the H4 Arg78 residue. In contrast, the other TSH2B-specific amino-acid residues did not induce any significant local structural changes in the TSH2B nucleosome. These findings may provide important information for understanding how testis-specific histone variants form nucleosomes during spermatogenesis.

Articles - 3wkj mentioned but not cited (1)

  1. Structure of human nucleosome containing the testis-specific histone variant TSH2B. Urahama T, Horikoshi N, Osakabe A, Tachiwana H, Kurumizaka H. Acta Crystallogr F Struct Biol Commun 70 444-449 (2014)


Reviews citing this publication (5)

  1. Essential Role of Histone Replacement and Modifications in Male Fertility. Wang T, Gao H, Li W, Liu C. Front Genet 10 962 (2019)
  2. The right place at the right time: chaperoning core histone variants. Mattiroli F, D'Arcy S, Luger K. EMBO Rep 16 1454-1466 (2015)
  3. Histone variants: essential actors in male genome programming. Hoghoughi N, Barral S, Vargas A, Rousseaux S, Khochbin S. J Biochem 163 97-103 (2018)
  4. Plant Histone HTB (H2B) Variants in Regulating Chromatin Structure and Function. Khadka J, Pesok A, Grafi G. Plants (Basel) 9 E1435 (2020)
  5. Structural studies of functional nucleosome complexes with transacting factors. Kurumizaka H. Proc Jpn Acad Ser B Phys Biol Sci 98 1-14 (2022)

Articles citing this publication (6)

  1. A method for evaluating nucleosome stability with a protein-binding fluorescent dye. Taguchi H, Horikoshi N, Arimura Y, Kurumizaka H. Methods 70 119-126 (2014)
  2. Comprehensive nucleosome interactome screen establishes fundamental principles of nucleosome binding. Skrajna A, Goldfarb D, Kedziora KM, Cousins EM, Grant GD, Spangler CJ, Barbour EH, Yan X, Hathaway NA, Brown NG, Cook JG, Major MB, McGinty RK. Nucleic Acids Res 48 9415-9432 (2020)
  3. Structural and functional analyses of nucleosome complexes with mouse histone variants TH2a and TH2b, involved in reprogramming. Padavattan S, Shinagawa T, Hasegawa K, Kumasaka T, Ishii S, Kumarevel T. Biochem Biophys Res Commun 464 929-935 (2015)
  4. Novel Classes and Evolutionary Turnover of Histone H2B Variants in the Mammalian Germline. Raman P, Rominger MC, Young JM, Molaro A, Tsukiyama T, Malik HS. Mol Biol Evol 39 msac019 (2022)
  5. Differential localization of histone variant TH2B during the first round compared with subsequent rounds of spermatogenesis. Beedle MT, Topping T, Hogarth C, Griswold M. Dev Dyn 248 488-500 (2019)
  6. Identification of the amino acid residues responsible for stable nucleosome formation by histone H3.Y. Kujirai T, Horikoshi N, Xie Y, Taguchi H, Kurumizaka H. Nucleus 8 239-248 (2017)


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