Cleavage profiles of tobacco etch virus (TEV)-derived substrates mediated by precursor and processed forms of the TEV NIa proteinase

References

1. Carrington J. C., Dougherty W. G. 1987a; Small nuclear inclusion protein encoded by a plant potyvirus genome is a protease. Journal of Virology 61:2540–2548
   [Google Scholar]
2. Carrington J. C., Dougherty W. G. 1987b; Processing of the tobacco etch virus 49K protease requires autoproteolysis. Virology 160:355–362
   [Google Scholar]
3. Carrington J. C., Parks T. D., Cary S. M., Doughery W. G. 1987; Vectors for cell-free expression and mutagenesis of protein coding sequences. Nucleic Acids Research 15:1006b
   [Google Scholar]
4. Carrington J. C., Cary S. M., Dougherty W. G. 1988; Mutational analysis of tobacco etch virus polyprotein processing: cis and trans proteolytic activities of polyproteins containing the 49-kilodalton proteinases. Journal of Virology 62:2313–2320
   [Google Scholar]
5. Carrington J. C., Cary S. M., Parks T. D., Dougherty W. G. 1989; A second proteinase encoded by a plant potyvirus genome. EM BO Journal 8:365–370
   [Google Scholar]
6. Dougherty W. G., Carrington J. C. 1988; Expression and function of potyviral gene products. Annual Review of Phytopathology 26:123–143
   [Google Scholar]
7. Dougherty W. G., Hiebert E. 1980; Translation of potyviral RNA in a rabbit reticulocyte lysate: identification of nuclear inclusion protein as products of tobacco etch virus RNA translation and cytoplasmic inclusion protein as a product of the potyvirus genome. Virology 104:174–182
   [Google Scholar]
8. Dougherty W. G., Parks T. D. 1989; Molecular genetic and biochemical evidence for the involvement of the heptapeptide cleavage sequence in determining the reaction profile at two tobacco etch virus cleavage sites in cell-free assays. Virology 172:145–155
   [Google Scholar]
9. Dougherty W. G., Parks T. D. 1991; Post-translational processing of the tobacco etch virus 49-kDa small nuclear inclusion protein: identification of an internal cleavage site and delimitation of VPg and proteinase domains. Virology 183:449–456
   [Google Scholar]
10. Dougherty W. G., Cary S. M., Parks T. D. 1989; Molecular genetic analysis of a plant virus polyprotein cleavage site: a model. Virology 171:356–364
    [Google Scholar]
11. Erlich H. A. (editor) 1989 PCR Technology: Principles and Applications for DNA Amplification New York: Stockton Press;
    [Google Scholar]
12. Harris K. S., Hellen C.U.T., Wimmer E. 1990; Proteolytic processing in the replication of picornaviruses. Seminars in Virology 1:323–333
    [Google Scholar]
13. Jore J., De Geus B., Jackson R. J., Pouwels P. H., Enger-Valk B. E. 1988; Poliovirus protein 3CD is the active protease for processing of the precursor protein P1 in vitro. Journal of General Virology 69:1627–1636
    [Google Scholar]
14. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227:680–685
    [Google Scholar]
15. Laín S., Riechmann J. L., García J. A. 1989; The complete nucleotide sequence of plum pox potyvirus RNA. Virus Research 13:157–172
    [Google Scholar]
16. Laín S., Riechmann J. L., García J. A. 1990; RNA helicase: a novel activity associated with a protein encoded by a positive strand RNA virus. Nucleic Acids Research 18:7003–7008
    [Google Scholar]
17. Murphy J. F., Rhoads R. E., Hunt A. G., Shaw J. G. 1990; The VPg of tobacco etch virus is the 49-kDa proteinase or the N-terminal 24-kDa part of the proteinase. Virology 178:285–288
    [Google Scholar]
18. Nicklin M. J. H., Harris K. S., Pallai P. V., Wimmer E. 1988; Poliovirus 3C: large-scale expression, purification, and specific cleavage activity on natural and synthetic substrates in vitro. Journal of Virology 62:4586–4593
    [Google Scholar]
19. Palmenberg A. C. 1990; Proteolytic processing of picornaviral polyprotein. Annual Review of Microbiology 44:603–623
    [Google Scholar]
20. Sambrook J., Fritsch E. F., Maniatis T. 1989 Molecular Cloning: A Laboratory Manual 2nd edn New York: Cold Spring Harbor Laboratory;
    [Google Scholar]
21. SAS Institute 1989 SAS/STAT User’s Guide Version 6, 4th edn. vol 1: pp 209–244 Cary: SAS Institute;
    [Google Scholar]
22. Strauss J. H., Strauss E. G. 1990; Alphavirus proteinases. Seminars in Virology 1:347–356
    [Google Scholar]
23. Taylor J. W., Schmidt W., Cosstick R., Okruszek A., Eckstein F. 1985a; The use of phosphorothioate–modified DNA in restriction enzyme reactions to prepare nicked DNA. Nucleic Acids Research 13:8749–8764
    [Google Scholar]
24. Taylor J. W., Ott J., Eckstein F. 1985b; The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA. Nucleic Acids Research 13:8765–8785
    [Google Scholar]
25. Vos P., Verver J., Jaegle M., Wellink J., van Kammen A., Goldbach R. 1988; Two viral proteins involved in the proteolytic processing of the cowpea mosaic virus polyproteins. Nucleic Acids Research 16:1967–1985
    [Google Scholar]
26. Ypma-Wong M. F., Semler B. 1987; Processing determinants required for in vitro cleavage of the poliovirus P1 precursor to capsid proteins. Journal of Virology 61:3181–3189
    [Google Scholar]
27. Ypma-Wong M. F., Dewalt P. G., Johnson V. H., Lamb J. G., Semler B. L. 1988; Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor. Virology 166:265–270
    [Google Scholar]