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Volumn 275, Issue 16, 2008, Pages 4152-4163

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

Author keywords

Coronavirus; Nucleocapsid protein; Phosphorylation; RS domain; Stress granules

Indexed keywords

ARGININE; DIPEPTIDE DERIVATIVE; NUCLEOCAPSID PROTEIN; PROTEIN SERINE KINASE; RIBONUCLEOPROTEIN; SERINE;

EID: 48249105910     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06564.x     Document Type: Article
Times cited : (120)

References (50)
  • 4
    • 0030633479 scopus 로고    scopus 로고
    • The molecular biology of coronaviruses
    • Lai MM Cavanagh D (1997) The molecular biology of coronaviruses. Adv Virus Res 48, 1 100.
    • (1997) Adv Virus Res , vol.48 , pp. 1-100
    • Lai, M.M.1    Cavanagh, D.2
  • 5
    • 0347319103 scopus 로고    scopus 로고
    • Sequence motifs involved in the regulation of discontinuous coronavirus subgenomic RNA synthesis
    • Zuniga S, Sola I, Alonso S Enjuanes L (2004) Sequence motifs involved in the regulation of discontinuous coronavirus subgenomic RNA synthesis. J Virol 78, 980 994.
    • (2004) J Virol , vol.78 , pp. 980-994
    • Zuniga, S.1    Sola, I.2    Alonso, S.3    Enjuanes, L.4
  • 6
    • 33748467621 scopus 로고    scopus 로고
    • Understanding the accessory viral proteins unique to the severe acute respiratory syndrome (SARS) coronavirus
    • Tan YJ, Lim SG Hong W (2006) Understanding the accessory viral proteins unique to the severe acute respiratory syndrome (SARS) coronavirus. Antiviral Res 72, 78 88.
    • (2006) Antiviral Res , vol.72 , pp. 78-88
    • Tan, Y.J.1    Lim, S.G.2    Hong, W.3
  • 7
    • 0028915630 scopus 로고
    • Quantification of individual subgenomic mRNA species during replication of the coronavirus transmissible gastroenteritis virus
    • Hiscox JA, Cavanagh D Britton P (1995) Quantification of individual subgenomic mRNA species during replication of the coronavirus transmissible gastroenteritis virus. Virus Res 36, 119 130.
    • (1995) Virus Res , vol.36 , pp. 119-130
    • Hiscox, J.A.1    Cavanagh, D.2    Britton, P.3
  • 8
    • 0029979024 scopus 로고    scopus 로고
    • The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins
    • Risco C, Anton IM, Enjuanes L Carrascosa JL (1996) The transmissible gastroenteritis coronavirus contains a spherical core shell consisting of M and N proteins. J Virol 70, 4773 4777.
    • (1996) J Virol , vol.70 , pp. 4773-4777
    • Risco, C.1    Anton, I.M.2    Enjuanes, L.3    Carrascosa, J.L.4
  • 10
    • 34147113199 scopus 로고    scopus 로고
    • 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 (2007) Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA. J Mol Biol 368, 1075 1086.
    • (2007) J Mol Biol , vol.368 , pp. 1075-1086
    • Chen, C.Y.1    Chang, C.K.2    Chang, Y.W.3    Sue, S.C.4    Bai, H.I.5    Riang, L.6    Hsiao, C.D.7    Huang, T.H.8
  • 11
    • 0029981390 scopus 로고    scopus 로고
    • Infectious bronchitis virus nucleocapsid protein binds RNA sequences in the 3′ terminus of the genome
    • Zhou ML, Williams AK, Chung SI, Wang L Collisson EW (1996) Infectious bronchitis virus nucleocapsid protein binds RNA sequences in the 3′ terminus of the genome. Virology 217, 191 199.
    • (1996) Virology , vol.217 , pp. 191-199
    • Zhou, M.L.1    Williams, A.K.2    Chung, S.I.3    Wang, L.4    Collisson, E.W.5
  • 12
    • 0033957603 scopus 로고    scopus 로고
    • High affinity interaction between nucleocapsid protein and leader/intergenic sequence of mouse hepatitis virus RNA
    • Nelson GW, Stohlman SA Tahara SM (2000) High affinity interaction between nucleocapsid protein and leader/intergenic sequence of mouse hepatitis virus RNA. J Gen Virol 81, 181 188.
    • (2000) J Gen Virol , vol.81 , pp. 181-188
    • Nelson, G.W.1    Stohlman, S.A.2    Tahara, S.M.3
  • 13
    • 0034032723 scopus 로고    scopus 로고
    • The amino and carboxyl domains of the infectious bronchitis virus nucleocapsid protein interact with 3′ genomic RNA
    • Zhou M Collisson EW (2000) The amino and carboxyl domains of the infectious bronchitis virus nucleocapsid protein interact with 3′ genomic RNA. Virus Res 67, 31 39.
    • (2000) Virus Res , vol.67 , pp. 31-39
    • Zhou, M.1    Collisson, E.W.2
  • 15
    • 0029872237 scopus 로고    scopus 로고
    • Cis requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication
    • Chang RY Brian DA (1996) Cis requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication. J Virol 70, 2201 2207.
    • (1996) J Virol , vol.70 , pp. 2201-2207
    • Chang, R.Y.1    Brian, D.A.2
  • 16
    • 0033799819 scopus 로고    scopus 로고
    • The arterivirus replicase is the only viral protein required for genome replication and subgenomic mRNA transcription
    • Molenkamp R, van Tol H, Rozier BCD, van der Meer Y, Spaan WJM Snijder EJ (2000) The arterivirus replicase is the only viral protein required for genome replication and subgenomic mRNA transcription. J Gen Virol 81, 2491 2496.
    • (2000) J Gen Virol , vol.81 , pp. 2491-2496
    • Molenkamp, R.1    Van Tol, H.2    Rozier, B.C.D.3    Van Der Meer, Y.4    Spaan, W.J.M.5    Snijder, E.J.6
  • 17
  • 18
    • 47049088603 scopus 로고    scopus 로고
    • Nucleocapsid protein of SARS-CoV inhibits cell cytokinesis and proliferation by interacting with translation elongation factor 1α
    • Zhou B, Wang Q, Liu X, Li P, Ma Q Cao C (2008) Nucleocapsid protein of SARS-CoV inhibits cell cytokinesis and proliferation by interacting with translation elongation factor 1α. J Virol 82, 6962 6971.
    • (2008) J Virol , vol.82 , pp. 6962-6971
    • Zhou, B.1    Wang, Q.2    Liu, X.3    Li, P.4    Ma, Q.5    Cao, C.6
  • 19
    • 33744965088 scopus 로고    scopus 로고
    • The nucleocapsid protein of severe acute respiratory syndrome-coronavirus inhibits the activity of cyclin-cyclin-dependent kinase complex and blocks S phase progression in mammalian cells
    • Surjit M, Liu B, Chow VT Lal SK (2006) The nucleocapsid protein of severe acute respiratory syndrome-coronavirus inhibits the activity of cyclin-cyclin-dependent kinase complex and blocks S phase progression in mammalian cells. J Biol Chem 281, 10669 10681.
    • (2006) J Biol Chem , vol.281 , pp. 10669-10681
    • Surjit, M.1    Liu, B.2    Chow, V.T.3    Lal, S.K.4
  • 20
    • 34147183857 scopus 로고    scopus 로고
    • Cell cycle dependent nucleolar localization of the coronavirus nucleocapsid protein
    • Cawood R, Harrison SM, Dove BK, Reed ML Hiscox JA (2007) Cell cycle dependent nucleolar localization of the coronavirus nucleocapsid protein. Cell Cycle 6, 863 867.
    • (2007) Cell Cycle , vol.6 , pp. 863-867
    • Cawood, R.1    Harrison, S.M.2    Dove, B.K.3    Reed, M.L.4    Hiscox, J.A.5
  • 21
    • 0036238652 scopus 로고    scopus 로고
    • Interaction of the coronavirus nucleoprotein with nucleolar antigens and the host cell
    • Chen H, Wurm T, Britton P, Brooks G Hiscox JA (2002) Interaction of the coronavirus nucleoprotein with nucleolar antigens and the host cell. J Virol 76, 5233 5250.
    • (2002) J Virol , vol.76 , pp. 5233-5250
    • Chen, H.1    Wurm, T.2    Britton, P.3    Brooks, G.4    Hiscox, J.A.5
  • 23
    • 28844505975 scopus 로고    scopus 로고
    • The nucleocapsid protein of coronavirus infectious bronchitis virus: Crystal structure of its N-terminal domain and multimerization properties
    • Fan H, Ooi A, Tan YW, Wang S, Fang S, Liu DX Lescar J (2005) The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties. Structure 13, 1859 1868.
    • (2005) Structure , vol.13 , pp. 1859-1868
    • Fan, H.1    Ooi, A.2    Tan, Y.W.3    Wang, S.4    Fang, S.5    Liu, D.X.6    Lescar, J.7
  • 24
    • 33750208365 scopus 로고    scopus 로고
    • Amino acid residues critical for RNA-binding in the N-terminal domain of the nucleocapsid protein are essential determinants for the infectivity of coronavirus in cultured cells
    • Tan YW, Fang S, Fan H, Lescar J Liu DX (2006) Amino acid residues critical for RNA-binding in the N-terminal domain of the nucleocapsid protein are essential determinants for the infectivity of coronavirus in cultured cells. Nucleic Acids Res 34, 4816 4825.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4816-4825
    • Tan, Y.W.1    Fang, S.2    Fan, H.3    Lescar, J.4    Liu, D.X.5
  • 25
    • 11144227044 scopus 로고    scopus 로고
    • Mass spectroscopic characterization of the coronavirus infectious bronchitis virus nucleoprotein and elucidation of the role of phosphorylation in RNA binding by using surface plasmon resonance
    • Chen H, Gill A, Dove BK, Emmett SR, Kemp CF, Ritchie MA, Dee M Hiscox JA (2005) Mass spectroscopic characterization of the coronavirus infectious bronchitis virus nucleoprotein and elucidation of the role of phosphorylation in RNA binding by using surface plasmon resonance. J Virol 79, 1164 1179.
    • (2005) J Virol , vol.79 , pp. 1164-1179
    • Chen, H.1    Gill, A.2    Dove, B.K.3    Emmett, S.R.4    Kemp, C.F.5    Ritchie, M.A.6    Dee, M.7    Hiscox, J.A.8
  • 26
    • 27944468304 scopus 로고    scopus 로고
    • RS-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization
    • Luo H, Ye F, Chen K, Shen X Jiang H (2005) RS-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization. Biochemistry 44, 15351 15358.
    • (2005) Biochemistry , vol.44 , pp. 15351-15358
    • Luo, H.1    Ye, F.2    Chen, K.3    Shen, X.4    Jiang, H.5
  • 27
    • 0029372979 scopus 로고
    • The superfamily of arginine/serine-rich splicing factors
    • Fu XD (1995) The superfamily of arginine/serine-rich splicing factors. RNA 1, 663 680.
    • (1995) RNA , vol.1 , pp. 663-680
    • Fu, X.D.1
  • 28
    • 0032737702 scopus 로고    scopus 로고
    • SR protein kinases: The splice of life
    • Stojdl DF Bell JC (1999) SR protein kinases: the splice of life. Biochem Cell Biol 77, 293 298.
    • (1999) Biochem Cell Biol , vol.77 , pp. 293-298
    • Stojdl, D.F.1    Bell, J.C.2
  • 29
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley BR (2000) Sorting out the complexity of SR protein functions. RNA 6, 1197 1211.
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 30
    • 0036785498 scopus 로고    scopus 로고
    • Phosphorylation of the porcine reproductive and respiratory syndrome virus nucleocapsid protein
    • Wootton SK, Rowland RR Yoo D (2002) Phosphorylation of the porcine reproductive and respiratory syndrome virus nucleocapsid protein. J Virol 76, 10569 10576.
    • (2002) J Virol , vol.76 , pp. 10569-10576
    • Wootton, S.K.1    Rowland, R.R.2    Yoo, D.3
  • 31
    • 34248168024 scopus 로고    scopus 로고
    • Identification of mouse hepatitis coronavirus A59 nucleocapsid protein phosphorylation sites
    • White TC, Yi Z Hogue BG (2007) Identification of mouse hepatitis coronavirus A59 nucleocapsid protein phosphorylation sites. Virus Res 126, 139 148.
    • (2007) Virus Res , vol.126 , pp. 139-148
    • White, T.C.1    Yi, Z.2    Hogue, B.G.3
  • 32
    • 23844529451 scopus 로고    scopus 로고
    • 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 (2005) The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation. J Virol 79, 11476 11486.
    • (2005) J Virol , vol.79 , pp. 11476-11486
    • Surjit, M.1    Kumar, R.2    Mishra, R.N.3    Reddy, M.K.4    Chow, V.T.5    Lal, S.K.6
  • 33
    • 23044516385 scopus 로고    scopus 로고
    • Phosphorylation and subcellular localization of transmissible gastroenteritis virus nucleocapsid protein in infected cells
    • Calvo E, Escors D, Lopez JA, Gonzalez JM, Alvarez A, Arza E Enjuanes L (2005) Phosphorylation and subcellular localization of transmissible gastroenteritis virus nucleocapsid protein in infected cells. J Gen Virol 86, 2255 2267.
    • (2005) J Gen Virol , vol.86 , pp. 2255-2267
    • Calvo, E.1    Escors, D.2    Lopez, J.A.3    Gonzalez, J.M.4    Alvarez, A.5    Arza, E.6    Enjuanes, L.7
  • 34
    • 0034751088 scopus 로고    scopus 로고
    • The coronavirus infectious bronchitis virus nucleoprotein localizes to the nucleolus
    • Hiscox JA, Wurm T, Wilson L, Britton P, Cavanagh D Brooks G (2001) The coronavirus infectious bronchitis virus nucleoprotein localizes to the nucleolus. J Virol 75, 506 512.
    • (2001) J Virol , vol.75 , pp. 506-512
    • Hiscox, J.A.1    Wurm, T.2    Wilson, L.3    Britton, P.4    Cavanagh, D.5    Brooks, G.6
  • 35
    • 0034849496 scopus 로고    scopus 로고
    • Localization to the nucleolus is a common feature of coronavirus nucleoproteins, and the protein may disrupt host cell division
    • Wurm T, Chen H, Hodgson T, Britton P, Brooks G Hiscox JA (2001) Localization to the nucleolus is a common feature of coronavirus nucleoproteins, and the protein may disrupt host cell division. J Virol 75, 9345 9356.
    • (2001) J Virol , vol.75 , pp. 9345-9356
    • Wurm, T.1    Chen, H.2    Hodgson, T.3    Britton, P.4    Brooks, G.5    Hiscox, J.A.6
  • 37
  • 38
    • 33745040231 scopus 로고    scopus 로고
    • Changes in nucleolar morphology and proteins during infection with the coronavirus infectious bronchitis virus
    • Dove BK, You JH, Reed ML, Emmett SR, Brooks G Hiscox JA (2006) Changes in nucleolar morphology and proteins during infection with the coronavirus infectious bronchitis virus. Cell Microbiol 8, 1147 1157.
    • (2006) Cell Microbiol , vol.8 , pp. 1147-1157
    • Dove, B.K.1    You, J.H.2    Reed, M.L.3    Emmett, S.R.4    Brooks, G.5    Hiscox, J.A.6
  • 39
    • 33745026452 scopus 로고    scopus 로고
    • Delineation and modeling of a nucleolar retention signal in the coronavirus nucleocapsid protein
    • Reed ML, Dove BK, Jackson RM, Collins R, Brooks G Hiscox JA (2006) Delineation and modeling of a nucleolar retention signal in the coronavirus nucleocapsid protein. Traffic 7, 833 848.
    • (2006) Traffic , vol.7 , pp. 833-848
    • Reed, M.L.1    Dove, B.K.2    Jackson, R.M.3    Collins, R.4    Brooks, G.5    Hiscox, J.A.6
  • 40
    • 0036863320 scopus 로고    scopus 로고
    • Stress granules: Sites of mRNA triage that regulate mRNA stability and translatability
    • Kedersha N Anderson P (2002) Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Biochem Soc Trans 30, 963 969.
    • (2002) Biochem Soc Trans , vol.30 , pp. 963-969
    • Kedersha, N.1    Anderson, P.2
  • 44
    • 34547883878 scopus 로고    scopus 로고
    • Mouse hepatitis coronavirus replication induces host translational shutoff and mRNA decay, with concomitant formation of stress granules and processing bodies
    • Raaben M, Groot Koerkamp MJ, Rottier PJ de Haan CA (2007) Mouse hepatitis coronavirus replication induces host translational shutoff and mRNA decay, with concomitant formation of stress granules and processing bodies. Cell Microbiol 9, 2218 2229.
    • (2007) Cell Microbiol , vol.9 , pp. 2218-2229
    • Raaben, M.1    Groot Koerkamp, M.J.2    Rottier, P.J.3    De Haan, C.A.4
  • 45
    • 27944504368 scopus 로고    scopus 로고
    • Dephosphorylation shows SR protein the way out
    • Scott AT Julio AA (2005) Dephosphorylation shows SR protein the way out. Molecular Cell 20, 499 501.
    • (2005) Molecular Cell , vol.20 , pp. 499-501
    • Scott, A.T.1    Julio, A.A.2
  • 46
    • 0036556757 scopus 로고    scopus 로고
    • Visibly stressed: The role of eIF2, TIA-1, and stress granules in protein translation
    • Anderson P Kedersha N (2002) Visibly stressed: the role of eIF2, TIA-1, and stress granules in protein translation. Cell Stress Chaperones 7, 213 221.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 213-221
    • Anderson, P.1    Kedersha, N.2
  • 47
    • 0039550795 scopus 로고    scopus 로고
    • A human papillomavirus E2 transcriptional activator: The interactions with cellular splicing factors and potential function in pre-mRNA processing
    • Lai MC, Teh BH Tarn WY (1999) A human papillomavirus E2 transcriptional activator: the interactions with cellular splicing factors and potential function in pre-mRNA processing. J Biol Chem 274, 11832 11841.
    • (1999) J Biol Chem , vol.274 , pp. 11832-11841
    • Lai, M.C.1    Teh, B.H.2    Tarn, W.Y.3
  • 48
    • 0036318795 scopus 로고    scopus 로고
    • Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein
    • Daub H, Blencke S, Habenberger P, Kurtenbach A, Dennenmoser J, Wissing J, Ullrich A Cotton M (2002) Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein. J Virol 76, 8124 8137.
    • (2002) J Virol , vol.76 , pp. 8124-8137
    • Daub, H.1    Blencke, S.2    Habenberger, P.3    Kurtenbach, A.4    Dennenmoser, J.5    Wissing, J.6    Ullrich, A.7    Cotton, M.8
  • 50
    • 23844546216 scopus 로고    scopus 로고
    • Intracellular localization of the severe acute respiratory syndrome coronavirus nucleocapsid protein: Absence of nucleolar accumulation during infection and after expression as a recombinant protein in vero cells
    • Rowland RR, Chauhan V, Fang Y, Pekosz A, Kerrigan M Burton MD (2005) Intracellular localization of the severe acute respiratory syndrome coronavirus nucleocapsid protein: absence of nucleolar accumulation during infection and after expression as a recombinant protein in vero cells. J Virol 79, 11507 11512.
    • (2005) J Virol , vol.79 , pp. 11507-11512
    • Rowland, R.R.1    Chauhan, V.2    Fang, Y.3    Pekosz, A.4    Kerrigan, M.5    Burton, M.D.6


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