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Chemical Synthesis of K34-Ubiquitylated H2B for Nucleosome Reconstitution and Single-Particle Cryo-Electron Microscopy Structural Analysis.
Li, Jiabin; He, Qiaoqiao; Liu, Yuntao; Liu, Sanling; Tang, Shan; Li, Chengmin; Sun, Demeng; Li, Xiaorun; Zhou, Min; Zhu, Ping; Bi, Guoqiang; Zhou, Zhenghong; Zheng, Ji-Shen; Tian, Changlin.
Afiliación
  • Li J; Key Laboratory of Bioorganic Phosphorus Chemistry, Chemical Biology, Ministry of Education), Department of Chemistry and School of Life Sciences, Tsinghua University, Beijing, 100084, China.
  • He Q; Hefei National Laboratory of Physical Sciences at MicroScale and, School of Life Sciences, University of Science and Technology of China and, High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, 230027, China.
  • Liu Y; Key Laboratory of Bioorganic Phosphorus Chemistry, Chemical Biology, Ministry of Education), Department of Chemistry and School of Life Sciences, Tsinghua University, Beijing, 100084, China.
  • Liu S; Hefei National Laboratory of Physical Sciences at MicroScale and, School of Life Sciences, University of Science and Technology of China and, High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, 230027, China.
  • Tang S; Hefei National Laboratory of Physical Sciences at MicroScale and, School of Life Sciences, University of Science and Technology of China and, High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, 230027, China.
  • Li C; Key Laboratory of Bioorganic Phosphorus Chemistry, Chemical Biology, Ministry of Education), Department of Chemistry and School of Life Sciences, Tsinghua University, Beijing, 100084, China.
  • Sun D; Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
  • Li X; Hefei National Laboratory of Physical Sciences at MicroScale and, School of Life Sciences, University of Science and Technology of China and, High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, 230027, China.
  • Zhou M; Hefei National Laboratory of Physical Sciences at MicroScale and, School of Life Sciences, University of Science and Technology of China and, High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, 230027, China.
  • Zhu P; Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
  • Bi G; Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
  • Zhou Z; Hefei National Laboratory of Physical Sciences at MicroScale and, School of Life Sciences, University of Science and Technology of China and, High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, 230027, China.
  • Zheng JS; Hefei National Laboratory of Physical Sciences at MicroScale and, School of Life Sciences, University of Science and Technology of China and, High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, 230027, China.
  • Tian C; Department of Microbiology, Immunology and Molecular Genetics and, California NanoSystems Systems, University of California Los Angeles, Los Angeles, CA, 90095, USA.
Chembiochem ; 18(2): 176-180, 2017 Jan 17.
Article en En | MEDLINE | ID: mdl-27976477
ABSTRACT
Post-translational modifications (e.g., ubiquitylation) of histones play important roles in dynamic regulation of chromatin. Histone ubiquitylation has been speculated to directly influence the structure and dynamics of nucleosomes. However, structural information for ubiquitylated nucleosomes is still lacking. Here we report an alternative strategy for total chemical synthesis of homogenous histone H2B-K34-ubiquitylation (H2B-K34Ub) by using acid-cleavable auxiliary-mediated ligation of peptide hydrazides for site-specific ubiquitylation. Synthetic H2B-K34Ub was efficiently incorporated into nucleosomes and further used for single-particle cryo-electron microscopy (cryo-EM) imaging. The cryo-EM structure of the nucleosome containing H2B-K34Ub suggests that two flexible ubiquitin domains protrude between the DNA chains of the nucleosomes. The DNA chains around the H2B-K34 sites shift and provide more space for ubiquitin to protrude. These analyses indicated local and slight structural influences on the nucleosome with ubiquitylation at the H2B-K34 site.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Histonas / Nucleosomas Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2017 Tipo del documento: Article País de afiliación: China
Texto completo
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Histonas / Nucleosomas Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2017 Tipo del documento: Article País de afiliación: China