SUMO-p-N protein dimer binds genomic RNA

Stable Identifier
R-HSA-9684229
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Human SARS coronavirus
Compartment
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N protein is synthesized in the cytosol of the host cell and then moves adjacent to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane, where mature virions are assembled. The primary function of the SARS-CoV nucleocapsid (N) protein is to encapsulate the positive-strand 5'-capped genomic RNA into a nucleocapsid for export. Nucleocapsid formation is depends on multiple weak protein-protein and protein-RNA interactions (reviewed in Chang et al, 2014).
The SARS-CoV N protein has globular N-terminal and C-terminal domains separated by three intrinsically disordered regions (IDRs) (Chang et al, 2006; Chang et al, 2009). N protein forms a weak dimer in the absence of RNA mediated by residues in the middle and C-terminal IDR (He et al, 2004a; Luo et al, 2006; Chang et al, 2005; Surjit et al, 2004; Yu et al, 2005; Chang et al, 2006; Chang et al, 2013; Surjit and Lal, 2008). Positive residues in the middle IDR are subject to phosphorylation, which may affect the function of N (Surjit et al, 2005; Peng et al, 2008).
Binding of the genomic RNA to one or a small number of N-N dimers may be the initiating event in nucleocapsid formation. Both the NTD and the CTD of N have been shown to have RNA-binding activity (Huang et al, 2004a; Huang et al, 2004b; Chen et al, 2007; Chang et al, 2009; Takeda et al, 2008), and the IDRs seem likely to also contribute (Chang et al, 2009). These initial binding events may nucleate nucleocapsid formation through further recruitment of N protein dimers (reviewed in Chang et al, 2014).

Literature References
PubMed ID Title Journal Year
17002283 Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: self-association analysis and nucleic acid binding characterization

Luo, H, Chen, J, Chen, K, Shen, X, Jiang, H

Biochemistry 2006
16228284 Modular organization of SARS coronavirus nucleocapsid protein

Chang, CK, Sue, SC, Yu, TH, Hsieh, CM, Tsai, CK, Chiang, YC, Lee, SJ, Hsiao, HH, Wu, WJ, Chang, WL, Lin, CH, Huang, TH

J. Biomed. Sci. 2006
15147189 Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein

Huang, Q, Yu, L, Petros, AM, Gunasekera, A, Liu, Z, Xu, N, Hajduk, P, Mack, J, Fesik, SW, Olejniczak, ET

Biochemistry 2004
18561946 Solution structure of the c-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAIL-NMR method

Takeda, M, Chang, CK, Ikeya, T, G√ľntert, P, Chang, YH, Hsu, YL, Huang, TH, Kainosho, M

J. Mol. Biol. 2008
18456656 The molecular mechanism governing the oncogenic potential of SOX2 in breast cancer

Chen, Y, Shi, L, Zhang, L, Li, R, Liang, J, Yu, W, Sun, L, Yang, X, Wang, Y, Zhang, Y, Shang, Y

J. Biol. Chem. 2008
23717688 Transient oligomerization of the SARS-CoV N protein--implication for virus ribonucleoprotein packaging

Chang, CK, Chen, CM, Chiang, MH, Hsu, YL, Huang, TH

PLoS ONE 2013
15849181 Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain

Yu, IM, Gustafson, CL, Diao, J, Burgner, JW, Li, Z, Zhang, J, Chen, J

J. Biol. Chem. 2005
15020242 Analysis of multimerization of the SARS coronavirus nucleocapsid protein

He, R, Dobie, F, Ballantine, M, Leeson, A, Li, Y, Bastien, N, Cutts, T, Andonov, A, Cao, J, Booth, TF, Plummer, FA, Tyler, S, Baker, L, Li, X

Biochem. Biophys. Res. Commun. 2004
15094372 The nucleocapsid protein of the SARS coronavirus is capable of self-association through a C-terminal 209 amino acid interaction domain

Surjit, M, Liu, B, Kumar, P, Chow, VT, Lal, SK

Biochem. Biophys. Res. Commun. 2004
17881296 The SARS-CoV nucleocapsid protein: a protein with multifarious activities

Surjit, M, Lal, SK

Infect. Genet. Evol. 2008
16214138 The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure

Chang, CK, Sue, SC, Yu, TH, Hsieh, CM, Tsai, CK, Chiang, YC, Lee, SJ, Hsiao, HH, Wu, WJ, Chang, CF, Huang, TH

FEBS Lett. 2005
18631359 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

Peng, TY, Lee, KR, Tarn, WY

FEBS J. 2008
24418573 The SARS coronavirus nucleocapsid protein--forms and functions

Chang, CK, Hou, MH, Chang, CF, Hsiao, CD, Huang, TH

Antiviral Res. 2014
17379242 Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA

Chen, CY, Chang, CK, Chang, YW, Sue, SC, Bai, HI, Riang, L, Hsiao, CD, Huang, TH

J. Mol. Biol. 2007
16103198 The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation

Surjit, M, Kumar, R, Mishra, RN, Reddy, MK, Chow, VT, Lal, SK

J. Virol. 2005
19052082 Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging

Chang, CK, Hsu, YL, Chang, YH, Chao, FA, Wu, MC, Huang, YS, Hu, CK, Huang, TH

J. Virol. 2009
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Name Identifier Synonyms
severe acute respiratory syndrome 2945 SARS-CoV infection, SARS
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