The Unique N-terminal Domain of the Large Subunit of Herpes Simplex Virus Ribonucleotide Reductase Is Preferentially Sensitive to Proteolysis

References

1. Anderson K. P., Frink R. J., Devi G. B., Gaylord B. H., Costa R. H., Wagner E. K. 1981; Detailed characterization of the mRNA mapping in the HindIII fragment K region of the herpes simplex virus type 1 genome. Journal of Virology 37:1011–1027
   [Google Scholar]
2. Atherton E., Gait M. J., Sheppard R. C., Williams B. J. 1979; The polyamide method of solid phase peptide and oligonucleotide synthesis. Bioorganic Chemistry 8:351–370
   [Google Scholar]
3. Bacchetti S., Evelegh M. J., Muirhead B. 1986; Identification and separation of the two subunits of the herpes simplex virus ribonucleotide reductase. Journal of Virology 57:1177–1181
   [Google Scholar]
4. Baer R., Bankier A. T., Biggin M. D., Deininger P. L., Farrell P. J., Gibson T. J., Hatfull G., Hudson G. S., Satchwell S. C. 1984; DNA sequence and expression of the B95-8 Epstein-Barr virus genome. Nature, London 310:207–211
   [Google Scholar]
5. Bassiri R. M., Dvorak J., Utiger R. D. 1979; Thyrotropin-releasing hormone. In Methods of Hormone Radioimmunoassay46–47 Jaffe B. M., Behrman H. R. New York: Academic Press;
   [Google Scholar]
6. Bradford M. M. 1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72:248–254
   [Google Scholar]
7. Brown S. M., Ritchie D. A., Subak-Sharpe J. H. 1973; Genetic studies with herpes simplex virus type 1. The isolation of temperature-sensitive mutants, their arrangement into complementation groups and recombination analysis leading to a linkage map. Journal of General Virology 18:329–346
   [Google Scholar]
8. Cameron J. M., McDougall I., Marsden H. S., Preston V. G., Ryan D. M., Subak-Sharpe J. H. 1988; Ribonucleotide reductase encoded by herpes simplex virus is a determinant of the pathogenicity of the virus in mice and a valid antiviral target. Journal of General Virology 69:2607–2612
   [Google Scholar]
9. Caras I., Lewinson B. B., Farby W., Williams S. R., Martin D. W. jr 1985; Cloned mouse ribonucleotide reductase M2 cDNA reveals amino acid sequence homology with Escherichia coli and herpes ribonucleotide reductase. Journal of Biological Chemistry 260:7015–7022
   [Google Scholar]
10. Carlson J., Fuchs J. A., Messing I. 1984; Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon. Proceedings of the National Academy of SciencesU.S.A 81:4294–4297
    [Google Scholar]
11. Cohen G. H. 1972; Ribonucleotide reductase activity of synchronized KB cells infected with herpes simplex virus. Journal of Virology 9:408–409
    [Google Scholar]
12. Cohen E. A., Charron J., Perret J., Langelier Y. 1985; Herpes simplex virus ribonucleotide reductase induced in infected BHK-21/C13 cells: biochemical evidence for the existence of two non-identical subunits, H1 and H2. Journal of General Virology 66:733–745
    [Google Scholar]
13. Darling A. J., McKay E. M., Ingemarsson R., Preston V. G. 1988; Reconstitution of herpes simplex virus type 1 ribonucleotide reductase activity from the large and small subunits. Virus Genes 2:163–176
    [Google Scholar]
14. Davison A. J., Scott J. E. 1986; The complete DNA sequence of varicella-zoster virus. Journal of General Virology 67:1759–1816
    [Google Scholar]
15. Dingwall C., Laskey R. A. 1986; Protein import into cell nucleus. Annual Review of Cell Biology 2:367–390
    [Google Scholar]
16. Draper K. G., Frink R. J., Wagner E. K. 1982; Detailed characterisation of an apparently unspliced β herpes simplex virus type 1 gene mapping in the interior of another. Journal of Virology 43:1123–1128
    [Google Scholar]
17. Dutia B. M. 1983; Ribonucleotide reductase induced by herpes simplex virus has a virus-specified constituent. Journal of General Virology 64:513–521
    [Google Scholar]
18. Elledge S. J., Davis R. W. 1987; Identification and isolation of the gene encoding the small subunit of ribonucleotide reductase from Saccharomyces cerevisiae: DNA damage-inducible gene required for mitotic viability. Molecular and Cellular Biology 7:2783–2793
    [Google Scholar]
19. Eriksson S., Sjöberg B.-M. 1989; Ribonucleotide reductase. In Allosteric Enzymes189–217 Herve G. Boca Raton: CRC Press;
    [Google Scholar]
20. Frame M. C., Marsden H. S., Dutia B. M. 1985; The ribonucleotide reductase induced by herpes simplex virus type 1 involves minimally a complex of two polypeptides (136K and 38K). Journal of General Virology 66:1581–1587
    [Google Scholar]
21. Galloway D. A., Swain M. A. 1984; Organization of the left-hand end of the herpes simplex virus. 2 BglII N fragment. Journal of Virology 49:724–730
    [Google Scholar]
22. Galloway D. A., Goldstein L. C., Lewis J. B. 1982; Identification of proteins encoded by a fragment of herpes simplex virus type 2 DNA that has transforming activity. Journal of Virology 42:530–537
    [Google Scholar]
23. Gibson T., Stockwell P., Ginsberg M., Barrell B. 1984; Homology between two EBV early genes and HSV ribonucleotide reductase and 38K genes. Nucleic Acids Research 12:5087–5099
    [Google Scholar]
24. Huang A., Jacobi G., Haj-Ahmad Y., Bachetti S. 1988; Expression of the HSV-2 ribonucleotide reductase subunits in adenovirus vectors or stably transformed cells: restoration of enzymatic activity by reassociation of enzyme subunits in the absence of other HSV proteins. Virology 163:462–470
    [Google Scholar]
25. Hurd H. K., Roberts C. W., Roberts J. W. 1987; Identification of the gene for the yeast ribonucleotide reductase small subunit and its inducibility by methyl methanesulfonate. Molecular and Cellular Biology 7:3673–3677
    [Google Scholar]
26. Ingemarson R., Lankinen H. 1987; The herpes simplex virus type 1 ribonucleotide reductase is a tight complex of the type α ₂ β ₂ composed of 40k and 140k proteins, of which the latter shows multiple forms due to proteolysis. Virology 156:417–422
    [Google Scholar]
27. Kagan A., Glick M. 1979; Oxytocin. In Methods of Hormone Radioimmunoassay327–329 Jaffe B. M., Behrmann H. R. New York: Academic Press;
    [Google Scholar]
28. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227:680–685
    [Google Scholar]
29. Lammers M., Follmann H. 1983; The ribonucleotide reductases – a unique group of metalloenzymes essential for cell proliferation. Structure and Bonding 54:27–91
    [Google Scholar]
30. Macpherson I., Stoker M. G. 1962; Polyoma transformation of hamster cell clones – an investigation of genetic factors affecting cell competence. Virology 16:147–151
    [Google Scholar]
31. Marsden H. S., Crombie I. K., Subak-Sharpe J. H. 1976; Control of protein synthesis in herpesvirus-infected cells: analysis of the polypeptides induced by wild type and sixteen temperature-sensitive mutants of HSV strain 17. Journal of General Virology 31:347–372
    [Google Scholar]
32. Marsden H. S., Stow N. D., Preston V. G., Timbury M. C., Wilkie N. M. 1978; Physical mapping of herpes simplex virus-induced polypeptides. Journal of Virology 28:624–642
    [Google Scholar]
33. McGeoch D. J., Dalrymple M. A., Davison A. J., Dolan A., Frame M. C., McNab D., Perry L. J., Scott J. E., Taylor P. 1988; The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. Journal of General Virology 69:1531–1547
    [Google Scholar]
34. McLauchlan J., Clements J. B. 1982; A 3′ co-terminus of two early herpes simplex virus type 1 mRNA. Nucleic Acids Research 10:501–512
    [Google Scholar]
35. McLauchlan J., Clements J. B. 1983a; DNA sequence homology between two co-linear loci on the HSV genome which have different transforming abilities. EMBO Journal 2:1953–1961
    [Google Scholar]
36. McLauchlan J., Clements J. B. 1983b; Organization of the herpes simplex virus type 1 transcription unit encoding two early proteins with molecular weights of 140000 and 40000. Journal of General Virology 64:997–1006
    [Google Scholar]
37. Nikas I., McLauchlan J., Davison A. J., Taylor W. R., Clements J. B. 1986; Structural features of ribonucleotide reductase. Proteins: Structure, Function and Genetics 1:376–384
    [Google Scholar]
38. Paradis H., Gaudreau P., Brazeau P., Langelier Y. 1988; Mechanism of inhibition of herpes simplex virus (HSV) ribonucleotide reductase by a nonapeptide corresponding to the carboxyl terminus of its subunit 2. Journal of Biological Chemistry 263:16045–16050
    [Google Scholar]
39. Posnett D. N., McGrath H., Tam J. P. 1988; A novel method for producing anti-peptide antibodies. Journal of Biological Chemistry 263:1719–1725
    [Google Scholar]
40. Preston C. M. 1979; Abnormal properties of an immediate early polypeptide in cells infected with the herpes simplex virus type 1 mutant tsK. Journal of Virology 32:357–369
    [Google Scholar]
41. Preston V. G., Palfreyman J. W., Dutia B. M. 1984; Identification of a herpes simplex virus type 1 polypeptide which is a component of the virus-induced ribonucleotide reductase. Journal of General Virology 65:1457–1466
    [Google Scholar]
42. Reichard P. 1988; Interactions between deoxyribonucleotide and DNA synthesis. Annual Review of Biochemistry 57:349–374
    [Google Scholar]
43. Sheppard R. C. 1983; Continuous flow methods in organic synthesis. Chemistry in Britain 19:402–413
    [Google Scholar]
44. Sjöberg B.-M., Eriksson S., Jornvall H., Carlquist M., Eklund H. 1985; Protein B1 of ribonucleotide reductase. Direct analytical data and comparisons with data indirectly deduced from the nucleotide sequence of the Escherichia coli nrd A gene. European Journal of Biochemistry 150:423–427
    [Google Scholar]
45. Sjöberg B.-M., Hahne S., Mathews C. Z., Mathews C. K., Band K. N., Gait M. J. 1986; The bacteriophage T4 gene for the small subunit of ribonucleotide reductase contains an intron. EMBO Journal 5:2031–2036
    [Google Scholar]
46. Slabaugh M., Roseman N., Davis R., Mathews C. 1988; Vaccinia virus-encoded ribonucleotide reductase: sequence conservation of the gene for the small subunit and its amplification in hydroxyurea-resistant mutants. Journal of Virology 62:519–527
    [Google Scholar]
47. Standart N. M., Bray S. J., George E. L., Hunt T., Ruderman J. V. 1985; The small subunit of ribonucleotide reductase is encoded by one of the most abundant translationally regulated maternal mRNAs in clam and sea urchin eggs. Cell Biology 100:1968–1976
    [Google Scholar]
48. Swain M. A., Galloway D. A. 1986; Herpes simplex virus specifies two subunits of ribonucleotide reductase encoded by 3′ coterminal transcripts. Journal of Virology 57:802–808
    [Google Scholar]
49. Tam J. P. 1988; Synthetic peptide vaccine design: synthesis and properties of a high-density multiple antigenic peptide system. Proceedings of the National Academy of SciencesU.S.A 85:5409–5413
    [Google Scholar]
50. Thelander L., Reichard P. 1979; Reduction of ribonucleotides. Annual Review of Biochemistry 48:133–158
    [Google Scholar]
51. Towbin H., Staehelin T., Gordon J. 1979; Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of SciencesU.S.A 76:4350–4354
    [Google Scholar]
52. Walter G., Scheidtmann K.-H., Carbone A., Laudano A. P., Doolittle R. F. 1980; Antibodies specific for the carboxy- and amino-terminal regions of simian virus 40 large tumor antigen. Proceedings of the National Academy of SciencesU.S.A 77:5197–5200
    [Google Scholar]
53. Zieve G., Penman S. 1976; Small RNA species of the HeLa cell: metabolism and subcellular localization. Cell 8:19–31
    [Google Scholar]