Modular organization of SARS coronavirus nucleocapsid protein.
The SARS-CoV nucleocapsid (N) protein is a major antigen in severe acute respiratory syndrome. It binds to the viral RNA genome and forms the ribonucleoprotein core. The SARS-CoV N protein has also been suggested to be involved in other important functions in the viral life cycle. Here we show that the N protein consists of two non-interacting structural domains, the N-terminal RNA-binding domain (RBD) (residues 45-181) and the C-terminal dimerization domain (residues 248-365) (DD), surrounded by flexible linkers. The C-terminal domain exists exclusively as a dimer in solution. The flexible linkers are intrinsically disordered and represent potential interaction sites with other protein and protein-RNA partners. Bioinformatics reveal that other coronavirus N proteins could share the same modular organization. This study provides information on the domain structure partition of SARS-CoV N protein and insights into the differing roles of structured and disordered regions in coronavirus nucleocapsid proteins.
Chang
Chung-ke
CK
Institute of Biomedical Sciences, Academia Sinica, Nankang, Taipei, Taiwan, ROC.
Sue
Shih-Che
SC
Yu
Tsan-hung
TH
Hsieh
Chiu-Min
CM
Tsai
Cheng-Kun
CK
Chiang
Yen-Chieh
YC
Lee
Shin-jye
SJ
Hsiao
Hsin-hao
HH
Wu
Wen-Jin
WJ
Chang
Wei-Lun
WL
Lin
Chun-Hung
CH
Huang
Tai-huang
TH
D000595:Amino Acid Sequence; D000818:Animals; D000956:Antigens, Viral / Q000737:chemistry* / Q000235:genetics; D000086462:Coronavirus Nucleocapsid Proteins; D006801:Humans; D008969:Molecular Sequence Data; D019590:Nucleocapsid Proteins / Q000737:chemistry* / Q000235:genetics; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D000956:Antigens, Viral; D000086462:Coronavirus Nucleocapsid Proteins; D019590:Nucleocapsid Proteins; D010446:Peptide Fragments