TAILIEUCHUNG - Báo cáo khoa học: Phosphorylation of the arginine/serine dipeptide-rich motif of the severe acute respiratory syndrome coronavirus nucleocapsid protein modulates its multimerization, translation inhibitory activity and cellular localization

Coronavirus nucleocapsid protein is abundant in infected cells and partici-pates in viral RNA replication and transcription. The central domain of the nucleocapsid protein contains several arginine⁄serine (RS) dipeptides, the biological significance of which has not been well investigated. | ễFEBS Journal Phosphorylation of the arginine serine dipeptide-rich motif of the severe acute respiratory syndrome coronavirus nucleocapsid protein modulates its multimerization translation inhibitory activity and cellular localization Tsui-Yi Peng1 2 Kuan-Rong Lee2 and Woan-Yuh Tarn1 1 Institute of BiomedicalSciences Academia Sinica Taipei Taiwan 2 Institute of Molecular Medicine NationalTsing Hua University Hsin-Chu Taiwan Keywords coronavirus nucleocapsid protein phosphorylation RS domain stress granules Correspondence . Tarn Institute of Biomedical Sciences Academia Sinica 128 Academy Road Section 2 Nankang Taipei 11529 Taiwan Fax 886 2 2782 9142 Tel 886 2 2652 3052 E-mail wtarn@ Received 15 April 2008 revised 17 June 2008 accepted 19 June 2008 doi Coronavirus nucleocapsid protein is abundant in infected cells and participates in viral RNA replication and transcription. The central domain of the nucleocapsid protein contains several arginine serine RS dipeptides the biological significance of which has not been well investigated. In the present study we demonstrate that the severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated primarily within the RS-rich region in cells and by SR protein kinase 1 in vitro. The nucleo-capsid protein could suppress translation and its RS motif is essential for such an activity. Moreover phosphorylation of the RS motif could modulate the translation inhibitory activity of the nucleocapsid protein. We further found that RS motif phosphorylation did not significantly affect RNA binding of the nucleocapsid protein but impaired its multimer-ization ability. We observed that the nucleocapsid protein could translocate to cytoplasmic stress granules in response to cellular stress. Deletion or mutations of the RS motif enhanced stress granule localization of the nucleocapsid protein whereas overexpression of SR protein kinase 1 inhibited nucleocapsid .

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• medical knowledge
• medical research
• analysis of cytoplasmic
• oxidation
• Crystal structure
• bacteria
• hemoglobin
• medicine
• cell proliferation
• breast cancer
• chemical reaction
• gastric cancer
• hormone medicine
• tumor cells
• biochemical studies
• environmental medicine