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. 1983;2(11):1953–1961. doi: 10.1002/j.1460-2075.1983.tb01684.x

DNA sequence homology between two co-linear loci on the HSV genome which have different transforming abilities.

J McLauchlan, J B Clements
PMCID: PMC555393  PMID: 6315408

Abstract

A transcription unit at the herpes simplex virus (HSV) type 2 transforming region, mtr-2 (map coordinates 0.580-0.625), comprises two early, unspliced mRNAs of 4.5 kb and 1.2 kb which are 3' co-terminal; a region including that specifying the 1.2-kb mRNA has been sequenced. The putative translated portions of these two mRNAs do not overlap and this feature, together with the arrangement of the mRNAs, is similar to the apparently equivalent co-linear HSV-1 locus which however does not transform. A putative stem and loops structure containing a TATA box is located upstream from the 5' terminus of the 1.2-kb mRNA within the translated portion of the 4.5-kb mRNA. Evidence for the generation of this structure by intra-strand reassociation under our hybridisation conditions has been obtained and possibilities are that it may function as a transcription-activated promoter or as an RNA polymerase pause site. A comparison of the equivalent HSV-2 and HSV-1 regions reveals a conserved sequence downstream from the 3' co-terminus which is present at a similar location in many eukaryotic genes (consensus sequence YGTGTTYY). The overall sequence conservation at this transcription unit is high except for regions located at: (1) the untranslated leaders of the 1.2-kb mRNAs; (2) the N termini of the polypeptides specified by the HSV-2/HSV-1 1.2-kb mRNAs; (3) the intergenic region beyond the 3' co termini. Regions (2) and (3) are located within a transforming fragment of HSV-2. The possible significance of these data for HSV-mediated cell transformation is discussed.

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Selected References

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  1. Anderson K. P., Frink R. J., Devi G. B., Gaylord B. H., Costa R. H., Wagner E. K. Detailed characterization of the mRNA mapping in the HindIII fragment K region of the herpes simplex virus type 1 genome. J Virol. 1981 Mar;37(3):1011–1027. doi: 10.1128/jvi.37.3.1011-1027.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Berk A. J., Sharp P. A. Structure of the adenovirus 2 early mRNAs. Cell. 1978 Jul;14(3):695–711. doi: 10.1016/0092-8674(78)90252-0. [DOI] [PubMed] [Google Scholar]
  3. Busslinger M., Portmann R., Irminger J. C., Birnstiel M. L. Ubiquitous and gene-specific regulatory 5' sequences in a sea urchin histone DNA clone coding for histone protein variants. Nucleic Acids Res. 1980 Mar 11;8(5):957–977. doi: 10.1093/nar/8.5.957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Camacho A., Spear G. Transformation of hamster embryo fibroblasts by a specific fragment of the herpes simplex virus genome. Cell. 1978 Nov;15(3):993–1002. doi: 10.1016/0092-8674(78)90283-0. [DOI] [PubMed] [Google Scholar]
  5. Chase J. W., Richardson C. C. Exonuclease VII of Escherichia coli. Mechanism of action. J Biol Chem. 1974 Jul 25;249(14):4553–4561. [PubMed] [Google Scholar]
  6. Clements J. B., Watson R. J., Wilkie N. M. Temporal regulation of herpes simplex virus type 1 transcription: location of transcripts on the viral genome. Cell. 1977 Sep;12(1):275–285. doi: 10.1016/0092-8674(77)90205-7. [DOI] [PubMed] [Google Scholar]
  7. Corden J., Wasylyk B., Buchwalder A., Sassone-Corsi P., Kedinger C., Chambon P. Promoter sequences of eukaryotic protein-coding genes. Science. 1980 Sep 19;209(4463):1406–1414. doi: 10.1126/science.6251548. [DOI] [PubMed] [Google Scholar]
  8. Davison A. J., Wilkie N. M. Nucleotide sequences of the joint between the L and S segments of herpes simplex virus types 1 and 2. J Gen Virol. 1981 Aug;55(Pt 2):315–331. doi: 10.1099/0022-1317-55-2-315. [DOI] [PubMed] [Google Scholar]
  9. Denhardt D. T. A membrane-filter technique for the detection of complementary DNA. Biochem Biophys Res Commun. 1966 Jun 13;23(5):641–646. doi: 10.1016/0006-291x(66)90447-5. [DOI] [PubMed] [Google Scholar]
  10. Docherty J. J., Subak-Sharpe J. H., Preston C. M. Identification of a virus-specific polypeptide associated with a transforming fragment (BglII-N) of herpes simplex virus type 2 DNA. J Virol. 1981 Oct;40(1):126–132. doi: 10.1128/jvi.40.1.126-132.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Draper K. G., Frink R. J., Wagner E. K. Detailed characterization of an apparently unspliced beta herpes simplex virus type 1 gene mapping in the interior of another. J Virol. 1982 Sep;43(3):1123–1128. doi: 10.1128/jvi.43.3.1123-1128.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Dutia B. M. Ribonucleotide reductase induced by herpes simplex virus has a virus-specified constituent. J Gen Virol. 1983 Mar;64(Pt 3):513–521. doi: 10.1099/0022-1317-64-3-513. [DOI] [PubMed] [Google Scholar]
  13. Easton A. J., Clements J. B. Temporal regulation of herpes simplex virus type 2 transcription and characterization of virus immediate early mRNA's. Nucleic Acids Res. 1980 Jun 25;8(12):2627–2645. doi: 10.1093/nar/8.12.2627. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Galloway D. A., Goldstein L. C., Lewis J. B. Identification of proteins encoded by a fragment of herpes simplex virus type 2 DNA that has transforming activity. J Virol. 1982 May;42(2):530–537. doi: 10.1128/jvi.42.2.530-537.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Galloway D. A., McDougall J. K. The oncogenic potential of herpes simplex viruses: evidence for a 'hit-and-run' mechanism. Nature. 1983 Mar 3;302(5903):21–24. doi: 10.1038/302021a0. [DOI] [PubMed] [Google Scholar]
  16. Huszar D., Bacchetti S. Is ribonucleotide reductase the transforming function of herpes simplex virus 2? Nature. 1983 Mar 3;302(5903):76–79. doi: 10.1038/302076a0. [DOI] [PubMed] [Google Scholar]
  17. Jariwalla R. J., Aurelian L., Ts'o P. O. Tumorigenic transformation induced by a specific fragment of DNA from herpes simplex virus type 2. Proc Natl Acad Sci U S A. 1980 Apr;77(4):2279–2283. doi: 10.1073/pnas.77.4.2279. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Jenkins F. J., Howett M. K., Spector D. J., Rapp F. Detection by RNA blot hybridization of RNA sequences homologous to the BglII-N fragment of herpes simplex virus type 2 DNA. J Virol. 1982 Dec;44(3):1092–1096. doi: 10.1128/jvi.44.3.1092-1096.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Kudler L., Jones T. R., Russell R. J., Hyman R. W. Heteroduplex analysis of cloned fragments of herpes simplex virus DNAs. Virology. 1983 Jan 15;124(1):86–99. doi: 10.1016/0042-6822(83)90292-1. [DOI] [PubMed] [Google Scholar]
  20. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  21. McKnight S. L. The nucleotide sequence and transcript map of the herpes simplex virus thymidine kinase gene. Nucleic Acids Res. 1980 Dec 20;8(24):5949–5964. doi: 10.1093/nar/8.24.5949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. McLauchlan J., Clements J. B. A 3' co-terminus of two early herpes simplex virus type 1 mRNAs. Nucleic Acids Res. 1982 Jan 22;10(2):501–512. doi: 10.1093/nar/10.2.501. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. McLauchlan J., Clements J. B. Organization of the herpes simplex virus type 1 transcription unit encoding two early proteins with molecular weights of 140000 and 40000. J Gen Virol. 1983 May;64(Pt 5):997–1006. doi: 10.1099/0022-1317-64-5-997. [DOI] [PubMed] [Google Scholar]
  24. Proudfoot N. J., Brownlee G. G. 3' non-coding region sequences in eukaryotic messenger RNA. Nature. 1976 Sep 16;263(5574):211–214. doi: 10.1038/263211a0. [DOI] [PubMed] [Google Scholar]
  25. Reyes G. R., LaFemina R., Hayward S. D., Hayward G. S. Morphological transformation by DNA fragments of human herpesviruses: evidence for two distinct transforming regions in herpes simplex virus types 1 and 2 and lack of correlation with biochemical transfer of the thymidine kinase gene. Cold Spring Harb Symp Quant Biol. 1980;44(Pt 1):629–641. doi: 10.1101/sqb.1980.044.01.066. [DOI] [PubMed] [Google Scholar]
  26. Rigby P. W., Dieckmann M., Rhodes C., Berg P. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol. 1977 Jun 15;113(1):237–251. doi: 10.1016/0022-2836(77)90052-3. [DOI] [PubMed] [Google Scholar]
  27. Spandidos D. A., Paul J. Transfer of human globin genes to erythroleukemic mouse cells. EMBO J. 1982;1(1):15–20. doi: 10.1002/j.1460-2075.1982.tb01117.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Suh M. Characterization of a polypeptide present in herpes simplex virus type 2-transformed and -infected hamster embryo cells. J Virol. 1982 Mar;41(3):1095–1098. doi: 10.1128/jvi.41.3.1095-1098.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Taya Y., Devos R., Tavernier J., Cheroutre H., Engler G., Fiers W. Cloning and structure of the human immune interferon-gamma chromosomal gene. EMBO J. 1982;1(8):953–958. doi: 10.1002/j.1460-2075.1982.tb01277.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Twigg A. J., Sherratt D. Trans-complementable copy-number mutants of plasmid ColE1. Nature. 1980 Jan 10;283(5743):216–218. doi: 10.1038/283216a0. [DOI] [PubMed] [Google Scholar]
  31. Watson R. J., Preston C. M., Clements J. B. Separation and characterization of herpes simplex virus type 1 immediate-early mRNA's. J Virol. 1979 Jul;31(1):42–52. doi: 10.1128/jvi.31.1.42-52.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Weaver R. F., Weissmann C. Mapping of RNA by a modification of the Berk-Sharp procedure: the 5' termini of 15 S beta-globin mRNA precursor and mature 10 s beta-globin mRNA have identical map coordinates. Nucleic Acids Res. 1979 Nov 10;7(5):1175–1193. doi: 10.1093/nar/7.5.1175. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Weinberg G., Ullman B., Martin D. W., Jr Mutator phenotypes in mammalian cell mutants with distinct biochemical defects and abnormal deoxyribonucleoside triphosphate pools. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2447–2451. doi: 10.1073/pnas.78.4.2447. [DOI] [PMC free article] [PubMed] [Google Scholar]

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