Your browser doesn't support javascript.
loading
Initiation of Parental Genome Reprogramming in Fertilized Oocyte by Splicing Kinase SRPK1-Catalyzed Protamine Phosphorylation.
Gou, Lan-Tao; Lim, Do-Hwan; Ma, Wubin; Aubol, Brandon E; Hao, Yajing; Wang, Xin; Zhao, Jun; Liang, Zhengyu; Shao, Changwei; Zhang, Xuan; Meng, Fan; Li, Hairi; Zhang, Xiaorong; Xu, Ruiming; Li, Dangsheng; Rosenfeld, Michael G; Mellon, Pamela L; Adams, Joseph A; Liu, Mo-Fang; Fu, Xiang-Dong.
  • Gou LT; Department of Cellular and Molecular Medicine, Institute of Genomic Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
  • Lim DH; Department of Cellular and Molecular Medicine, Institute of Genomic Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
  • Ma W; Howard Hughes Medical Institute, Department of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
  • Aubol BE; Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093, USA.
  • Hao Y; Department of Cellular and Molecular Medicine, Institute of Genomic Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
  • Wang X; State Key Laboratory of Molecular Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences-University of Chinese Academy of Sciences, Shanghai 200031, China.
  • Zhao J; Transgenic and Knockout Mouse Core, University of California, San Diego, La Jolla, CA 92093, USA.
  • Liang Z; Department of Cellular and Molecular Medicine, Institute of Genomic Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
  • Shao C; Department of Cellular and Molecular Medicine, Institute of Genomic Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
  • Zhang X; Department of Cellular and Molecular Medicine, Institute of Genomic Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
  • Meng F; Department of Cellular and Molecular Medicine, Institute of Genomic Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
  • Li H; Department of Cellular and Molecular Medicine, Institute of Genomic Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
  • Zhang X; Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
  • Xu R; Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
  • Li D; Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China.
  • Rosenfeld MG; Howard Hughes Medical Institute, Department of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
  • Mellon PL; Transgenic and Knockout Mouse Core, University of California, San Diego, La Jolla, CA 92093, USA; Department of Obstetrics, Gynecology, and Reproductive Sciences, University of California, San Diego, La Jolla, CA 92093, USA.
  • Adams JA; Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093, USA.
  • Liu MF; State Key Laboratory of Molecular Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences-University of Chinese Academy of Sciences, Shanghai 200031, China.
  • Fu XD; Department of Cellular and Molecular Medicine, Institute of Genomic Medicine, University of California, San Diego, La Jolla, CA 92093, USA. Electronic address: xdfu@ucsd.edu.
Cell ; 180(6): 1212-1227.e14, 2020 03 19.
Article en En | MEDLINE | ID: mdl-32169215
ABSTRACT
The paternal genome undergoes a massive exchange of histone with protamine for compaction into sperm during spermiogenesis. Upon fertilization, this process is potently reversed, which is essential for parental genome reprogramming and subsequent activation; however, it remains poorly understood how this fundamental process is initiated and regulated. Here, we report that the previously characterized splicing kinase SRPK1 initiates this life-beginning event by catalyzing site-specific phosphorylation of protamine, thereby triggering protamine-to-histone exchange in the fertilized oocyte. Interestingly, protamine undergoes a DNA-dependent phase transition to gel-like condensates and SRPK1-mediated phosphorylation likely helps open up such structures to enhance protamine dismissal by nucleoplasmin (NPM2) and enable the recruitment of HIRA for H3.3 deposition. Remarkably, genome-wide assay for transposase-accessible chromatin sequencing (ATAC-seq) analysis reveals that selective chromatin accessibility in both sperm and MII oocytes is largely erased in early pronuclei in a protamine phosphorylation-dependent manner, suggesting that SRPK1-catalyzed phosphorylation initiates a highly synchronized reorganization program in both parental genomes.
Asunto(s)
Palabras clave
Texto completo
Imprimir
XML
PubMed Links
Search on Google

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Cromatina / Protaminas / Proteínas Serina-Treonina Quinasas Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Año: 2020 Tipo del documento: Article
Texto completo
Imprimir
XML
PubMed Links
Search on Google

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Cromatina / Protaminas / Proteínas Serina-Treonina Quinasas Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Año: 2020 Tipo del documento: Article