Sumoylation of the nucleocapsid protein of severe acute respiratory syndrome coronavirus

作者：Li FQS; Xiao H; Tam JP; Liu DX^*

来源：FEBS LETTERS, 2005, 579(11): 2387-2396.

DOI：10.1016/j.febslet.2005.03.039

• SARS-CoV
• nucleocapsid protein
• sumoylation
• oligomerization
• multinucleated cells
• cytokinesis

Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes a highly basic nucleocapsid (N) protein of 422 amino acids. Similar to other coronavirus N proteins, SARS-CoV N protein is predicted to be phosphorylated and SARS may contain nuclear localization signals, serine/arginine-rich motif, RNA binding domain and regions responsible for self-association and homo-oligomerization. In this study, we demonstrate that the protein is posttranslationally modified by covalent attachment to the small ubiquitin-like modifier. The major sumoylation site was mapped to the (62)lysine residue of the N protein. Further expression and characterization of wild type N protein and K62A mutant reveal that sumoylation of the N protein drastically promotes its homo-oligomerization, and plays certain roles in the N protein-mediated interference of host cell division. This is the first report showing that a coronavirus N protein undergoes posttranslational modification by sumoylation, and the functional implication of this modification in the formation of coronavirus ribouncleoprotein complex, virion assembly and virus-host interactions.

• 出版日期2005-4-25
• 单位南阳理工学院