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Crystal structures of heterotypic nucleosomes containing histones H2A.Z and H2A.

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Horikoshi N, Arimura Y, Taguchi H, Kurumizaka H
OpenAccess logo Open Biol 6 (2016)
Related entries: 5b31, 5b32

Cited: 20 times
EuropePMC logo PMID: 27358293

Abstract

H2A.Z is incorporated into nucleosomes located around transcription start sites and functions as an epigenetic regulator for the transcription of certain genes. During transcriptional regulation, the heterotypic H2A.Z/H2A nucleosome containing one each of H2A.Z and H2A is formed. However, previous homotypic H2A.Z nucleosome structures suggested that the L1 loop region of H2A.Z would sterically clash with the corresponding region of canonical H2A in the heterotypic nucleosome. To resolve this issue, we determined the crystal structures of heterotypic H2A.Z/H2A nucleosomes. In the H2A.Z/H2A nucleosome structure, the H2A.Z L1 loop structure was drastically altered without any structural changes of the canonical H2A L1 loop, thus avoiding the steric clash. Unexpectedly, the heterotypic H2A.Z/H2A nucleosome is more stable than the homotypic H2A.Z nucleosome. These data suggested that the flexible character of the H2A.Z L1 loop plays an essential role in forming the stable heterotypic H2A.Z/H2A nucleosome.

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  2. Improved Virus Isoelectric Point Estimation by Exclusion of Known and Predicted Genome-Binding Regions. Heffron J, Mayer BK. Appl Environ Microbiol 86 e01674-20 (2020)
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  1. Histone variants on the move: substrates for chromatin dynamics. Talbert PB, Henikoff S. Nat Rev Mol Cell Biol 18 115-126 (2017)
  2. The histone variant H2A.Z in gene regulation. Giaimo BD, Ferrante F, Herchenröther A, Hake SB, Borggrefe T. Epigenetics Chromatin 12 37 (2019)
  3. Structural diversity of the nucleosome. Koyama M, Kurumizaka H. J Biochem 163 85-95 (2018)
  4. H2A Variants in Arabidopsis: Versatile Regulators of Genome Activity. Lei B, Berger F. Plant Commun 1 100015 (2020)
  5. Histone variants and chromatin structure, update of advances. Sokolova V, Sarkar S, Tan D. Comput Struct Biotechnol J 21 299-311 (2023)
  6. How does chromatin package DNA within nucleus and regulate gene expression? Fazary AE, Ju YH, Abd-Rabboh HSM. Int J Biol Macromol 101 862-881 (2017)
  7. Janus Bioparticles: Asymmetric Nucleosomes and Their Preparation Using Chemical Biology Approaches. Mitchener MM, Muir TW. Acc Chem Res 54 3215-3227 (2021)

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  1. Single Amino Acid Change Underlies Distinct Roles of H2A.Z Subtypes in Human Syndrome. Greenberg RS, Long HK, Swigut T, Wysocka J. Cell 178 1421-1436.e24 (2019)
  2. Oncohistone mutations enhance chromatin remodeling and alter cell fates. Bagert JD, Mitchener MM, Patriotis AL, Dul BE, Wojcik F, Nacev BA, Feng L, Allis CD, Muir TW. Nat Chem Biol 17 403-411 (2021)
  3. Histone H2A variants confer specific properties to nucleosomes and impact on chromatin accessibility. Osakabe A, Lorkovic ZJ, Kobayashi W, Tachiwana H, Yelagandula R, Kurumizaka H, Berger F. Nucleic Acids Res 46 7675-7685 (2018)
  4. Structural basis of chromatin regulation by histone variant H2A.Z. Lewis TS, Sokolova V, Jung H, Ng H, Tan D. Nucleic Acids Res 49 11379-11391 (2021)
  5. The N-terminal and C-terminal halves of histone H2A.Z independently function in nucleosome positioning and stability. Sato S, Tanaka N, Arimura Y, Kujirai T, Kurumizaka H. Genes Cells 25 538-546 (2020)
  6. What makes a histone variant a variant: Changing H2A to become H2A.Z. Brewis HT, Wang AY, Gaub A, Lau JJ, Stirling PC, Kobor MS. PLoS Genet 17 e1009950 (2021)
  7. 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)
  8. Histone variants H3.3 and H2A.Z/H3.3 facilitate excision of uracil from nucleosome core particles. Li C, Rioux KL, Delaney S. DNA Repair (Amst) 116 103355 (2022)
  9. The P. falciparum alternative histones Pf H2A.Z and Pf H2B.Z are dynamically acetylated and antagonized by PfSir2 histone deacetylases at heterochromatin boundaries. Azizan S, Selvarajah SA, Tang J, Jeninga MD, Schulz D, Pareek K, Herr T, Day KP, De Koning-Ward TF, Petter M, Duffy MF. mBio e0201423 (2023)


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