Modular organization of SARS coronavirus nucleocapsid protein

Chung Ke Chang; Shih Che Sue; Tsan Hung Yu; Chiu Min Hsieh; Cheng Kun Tsai; Yen Chieh Chiang; Shin Jye Lee; Hsin Hao Hsiao; Wen Jin Wu; Wei Lun Chang; Chun Hung Lin; Tai Huang Huang

doi:10.1007/s11373-005-9035-9

Modular organization of SARS coronavirus nucleocapsid protein

Chung Ke Chang, Shih Che Sue, Tsan Hung Yu, Chiu Min Hsieh, Cheng Kun Tsai, Yen Chieh Chiang, Shin Jye Lee, Hsin Hao Hsiao, Wen Jin Wu, Wei Lun Chang, Chun Hung Lin, Tai Huang Huang^*

^*Corresponding author for this work

Department of Physics

Research output: Contribution to journal › Article › peer-review

241 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	59-72
Number of pages	14
Journal	Journal of Biomedical Science
Volume	13
Issue number	1
DOIs	https://doi.org/10.1007/s11373-005-9035-9
Publication status	Published - 2006 Jan

Keywords

Capsid protein
Coronavirus
Domain arrangement
Intrinsically disordered protein
NMR
Oligomerization
SARS

ASJC Scopus subject areas

Endocrinology, Diabetes and Metabolism
Molecular Biology
Clinical Biochemistry
Cell Biology
Biochemistry, medical
Pharmacology (medical)

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1007/s11373-005-9035-9

Cite this

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title = "Modular organization of SARS coronavirus nucleocapsid protein",

abstract = "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.",

keywords = "Capsid protein, Coronavirus, Domain arrangement, Intrinsically disordered protein, NMR, Oligomerization, SARS",

author = "Chang, {Chung Ke} and Sue, {Shih Che} and Yu, {Tsan Hung} and Hsieh, {Chiu Min} and Tsai, {Cheng Kun} and Chiang, {Yen Chieh} and Lee, {Shin Jye} and Hsiao, {Hsin Hao} and Wu, {Wen Jin} and Chang, {Wei Lun} and Lin, {Chun Hung} and Huang, {Tai Huang}",

note = "Funding Information: This work was supported in part by the Academia Sinica and by grants (NSC 92-2113-M-001-056 and NSC 92-2751-B-001-020-Y) (to THH) from the National Science Council of the Republic of China. The NMR spectra were obtained at the High-field Biomacromolecular NMR Core Facility, National Research Program for Genomic Medicine (NRPGM), Taiwan, Republic of China.",

year = "2006",

month = jan,

doi = "10.1007/s11373-005-9035-9",

language = "English",

volume = "13",

pages = "59--72",

journal = "Journal of Biomedical Science",

issn = "1021-7770",

publisher = "BioMed Central",

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T1 - Modular organization of SARS coronavirus nucleocapsid protein

AU - Chang, Chung Ke

AU - Sue, Shih Che

AU - Yu, Tsan Hung

AU - Hsieh, Chiu Min

AU - Tsai, Cheng Kun

AU - Chiang, Yen Chieh

AU - Lee, Shin Jye

AU - Hsiao, Hsin Hao

AU - Wu, Wen Jin

AU - Chang, Wei Lun

AU - Lin, Chun Hung

AU - Huang, Tai Huang

N1 - Funding Information: This work was supported in part by the Academia Sinica and by grants (NSC 92-2113-M-001-056 and NSC 92-2751-B-001-020-Y) (to THH) from the National Science Council of the Republic of China. The NMR spectra were obtained at the High-field Biomacromolecular NMR Core Facility, National Research Program for Genomic Medicine (NRPGM), Taiwan, Republic of China.

PY - 2006/1

Y1 - 2006/1

N2 - 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.

AB - 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.

KW - Capsid protein

KW - Coronavirus

KW - Domain arrangement

KW - Intrinsically disordered protein

KW - NMR

KW - Oligomerization

KW - SARS

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Modular organization of SARS coronavirus nucleocapsid protein

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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