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Molecular cell. 2020 Dec 17;80(6):1092-1103.e4. doi: 10.1016/j.molcel.2020.11.025 Q116.62025

Phosphoregulation of Phase Separation by the SARS-CoV-2 N Protein Suggests a Biophysical Basis for its Dual Functions

SARS-CoV-2 N蛋白的磷酸化调节其相分离并揭示了其双重功能的生物物理基础 翻译改进

Christopher R Carlson  1, Jonathan B Asfaha  1, Chloe M Ghent  2, Conor J Howard  3, Nairi Hartooni  1, Maliheh Safari  4, Alan D Frankel  3, David O Morgan  5

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作者单位

  • 1 Department of Physiology, University of California, San Francisco, San Francisco, CA 94143, USA; Tetrad Graduate Program, University of California, San Francisco, San Francisco, CA 94143, USA.
  • 2 Department of Physiology, University of California, San Francisco, San Francisco, CA 94143, USA.
  • 3 Department of Biochemistry & Biophysics, University of California, San Francisco, San Francisco, CA 94143, USA; Tetrad Graduate Program, University of California, San Francisco, San Francisco, CA 94143, USA.
  • 4 Department of Biochemistry & Biophysics, University of California, San Francisco, San Francisco, CA 94143, USA.
  • 5 Department of Physiology, University of California, San Francisco, San Francisco, CA 94143, USA; Tetrad Graduate Program, University of California, San Francisco, San Francisco, CA 94143, USA. Electronic address: david.morgan@ucsf.edu.

    • DOI: 10.1016/j.molcel.2020.11.025 PMID: 33248025

    摘要 Ai翻译

    The nucleocapsid (N) protein of coronaviruses serves two major functions: compaction of the RNA genome in the virion and regulation of viral gene transcription. It is not clear how the N protein mediates such distinct functions. The N protein contains two RNA-binding domains surrounded by regions of intrinsic disorder. Phosphorylation of the central disordered region promotes the protein's transcriptional function, but the underlying mechanism is not known. Here, we show that the N protein of SARS-CoV-2, together with viral RNA, forms biomolecular condensates. Unmodified N protein forms partially ordered gel-like condensates and discrete 15-nm particles based on multivalent RNA-protein and protein-protein interactions. Phosphorylation reduces these interactions, generating a more liquid-like droplet. We propose that distinct oligomeric states support the two functions of the N protein: unmodified protein forms a structured oligomer that is suited for nucleocapsid assembly, and phosphorylated protein forms a liquid-like compartment for viral genome processing.

    Keywords: COVID-19; Coronavirus; N protein; SARS-CoV-2; biomolecular condensate; nucleocapsid; phase separation; phosphorylation.

    Keywords：SARS-CoV-2 N protein; phosphoregulation; phase separation; dual functions

    关键词：SARS-CoV-2 N蛋白; 磷酸化调节; 相分离; 双重功能

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    期刊名：Molecular cell

    缩写：MOL CELL

    ISSN：1097-2765

    e-ISSN：1097-4164

    IF/分区：16.6/Q1

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    Phosphoregulation of Phase Separation by the SARS-CoV-2 N Protein Suggests a Biophysical Basis for its Dual Functions