Insights into SARS-CoV transcription and replication from the structure of the nsp7-nsp8 hexadecamer

Nature Structural and Molecular Biology

Volumn 12, Issue 11, 2005, Pages 980-986

  Zhai, Yujia ^a   Sun, Fei ^a   Li, Xuemei ^a,b   Pang, Hai ^a   Xu, Xiaoling ^a   Bartlam, Mark ^a   Rao, Zihe ^a,b  

^a TSINGHUA UNIVERSITY   (China)

^b INSTITUTE OF BIOPHYSICS   (China)

Author keywords

[No Author keywords available]

Indexed keywords

NONSTRUCTURAL PROTEIN 7; NONSTRUCTURAL PROTEIN 8; RNA; RNA POLYMERASE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ELECTRICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; OPTICAL RESOLUTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; SARS CORONAVIRUS; VIRUS REPLICATION; VIRUS TRANSCRIPTION;

AMINO ACID SEQUENCE; BASE SEQUENCE; CRYSTALLIZATION; DNA PRIMERS; ELECTROPHORETIC MOBILITY SHIFT ASSAY; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; RNA REPLICASE; SARS VIRUS; SEQUENCE ANALYSIS, DNA; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSCRIPTION, GENETIC; VIRAL NONSTRUCTURAL PROTEINS; VIRUS REPLICATION;

CORONAVIRUS; SARS CORONAVIRUS;

EID: 33645000761     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb999     Document Type: Article

References (42)

1. Brierley, I., Digard, P. & Inglis, S.C. Characterization of an efficient coronavirus ribosomal frameshifting signal: requirement for an RNA pseudoknot. Cell 57, 537-547 (1989).
2. Ziebuhr, J., Snijder, E.J. & Gorbalenya, A.E. Virus-encoded proteinases and proteolytic processing in the Nidovirales. J. Gen. Virol. 81, 853-879 (2000).
3. Thiel, V. et al. Mechanisms and enzymes involved in SARS coronavirus genome expression. J. Gen. Virol. 84, 2305-2315 (2003).
4. Marra, M.A. et al. The Genome sequence of the SARS-associated coronavirus. Science 300, 1399-1404 (2003).
5. Rota, P.A. et al. Characterization of a novel coronavirus associated with severe acute respiratory syndrome. Science 300, 1394-1399 (2003).
6. Snijder, E.J. et al. Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage. J. Mol. Biol. 331, 991-1004 (2003).
7. Gorbalenya, A.E. Big nidovirus genome. When count and order of domains matter. Adv. Exp. Med. Biol. 494, 1-17 (2001).
8. Drosten, C. et al. Identification of a novel coronavirus in patients with severe acute respiratory syndrome. N. Engl. J. Med. 348, 1967-1976 (2003).
9. Fouchier, R.A. et al. Aetiology: Koch's postulates fulfilled for SARS virus. Nature 423, 240 (2003).
10. Ksiazek, T.G. et al. A novel coronavirus associated with severe acute respiratory syndrome. N. Engl. J. Med. 348, 1953-1966 (2003).
11. Kuiken, T. et al. Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome. Lancet 362, 263-270 (2003).
12. Peiris, J.S. et al. Coronavirus as a possible cause of severe acute respiratory syndrome. Lancet 361, 1319-1325 (2003).
13. Peiris, J.S., Yuen, K.Y., Osterhaus, A.D. & Stohr, K. The severe acute respiratory syndrome. N. Engl. J. Med. 349, 2431-2441 (2003).
14. Zhao, Z. et al. Description and clinical treatment of an early outbreak of severe acute respiratory syndrome (SARS) in Guangzhou, PR China. J. Med. Microbiol. 52, 715-720 (2003).
15. Zhong, N.S. et al. Epidemiology and cause of severe acute respiratory syndrome (SARS) in Guangdong, People's Republic of China, in February, 2003. Lancet 362, 1353-1358 (2003).
16. Yang, H. et al. The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor. Proc. Natl. Acad. Sci. USA 100, 13190-13195 (2003).
17. Ivanov, K.A. et al. Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase. J. Virol. 78, 5619-5632 (2004).
18. Ivanov, K.A. et al. Major genetic marker of nidoviruses encodes a replicative endoribonuclease. Proc. Natl. Acad. Sci. USA 101, 12694-12699 (2004).
19. Egloff, M.P. et al. The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world. Proc. Natl. Acad. Sci. USA 101, 3792-3796 (2004).
20. Sutton, G. et al. The nsp9 replicase protein of SARS-coronavirus, structure and functional insights. Structure (Camb). 12, 341-353 (2004).
21. Woo, P.C. et al. Characterization and complete genome sequence of a novel coronavirus, coronavirus HKU1, from patients with pneumonia. J. Virol. 79, 884-895 (2005).
22. Holm, L. & Sander, C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20, 478-480 (1995).
23. Dunker, A.K., Brown, C.J., Lawson, J.D., lakoucheva, L.M. & Obradovic, Z. Intrinsic disorder and protein function. Biochemistry 41, 6573-6582 (2002).
24. Taylor, T.C. & Andersson, I. The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate. J. Mol. Biol. 265, 432-444 (1997).
25. Xu, Z., Horwich, A.L. & Sigler, P.B. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388, 741-750 (1997).
26. Kong, X.P., Onrust, R., O'Donnell, M. & Kuriyan, J. Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp. Cell 69, 425-437 (1992).
27. Krishna, T.S., Kong, X.P., Gary, S., Burgers, P.M. & Kuriyan, J. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell 79, 1233-1243 (1994).
28. Siddell, S.G. The coronaviridae: an introduction. in The Coronaviridae (ed. Siddell, S.G.) 1-9 (Plenum, New York, USA, 1995).
29. Bauer, G.A. & Burgers, P.M. The yeast analog of mammalian cyclin/proliferating-cell nuclear antigen interacts with mammalian DNA polymerase delta. Proc. Natl. Acad. Sci. USA 85, 7506-7510 (1988).
30. Brockway, S.M., Clay, C.T., Lu, X.T. & Denison, M.R. Characterization of the expression, intracellular localization, and replication complex association of the putative mouse hepatitis virus RNA-dependent RNA polymerase. J. Virol. 77, 10515-10527 (2003).
31. Bost, A.G., Carnahan, R.H., Lu, X.T. & Denison, M.R. Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly. J. Virol. 74, 3379-3387 (2000).
32. Doublie, S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276, 523-530 (1997).
33. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
34. Terwilliger, T.C. & Berendzen, J. Automated MAD and MIR structure solution. Acta Crystallogr. D Biol. Crystallogr. 55, 849-861 (1999).
35. Terwilliger, T.C. Maximum-likelihood density modification. Acta Crystallogr. D Biol. Crystallogr. 56, 965-972 (2000).
36. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-9 (1991).
37. Brunger, A.T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
38. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
39. Ludtke, S.J., Baldwin, P.R. & Chiu, W. EMAN: semiautomated software for high-resolution single particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
40. Esnouf, R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. 15, 132-134 (1997).
41. Thompson, J.D., Higgins, D.G. & Gibson, T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680 (1994).
42. Gouet, P., Courcelle, E., Stuart, D.I. & Metoz, F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15, 305-308 (1999).