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. 1991 Nov;65(11):5657–5662. doi: 10.1128/jvi.65.11.5657-5662.1991

Adenovirus virus-associated RNA and translation control.

M B Mathews 1, T Shenk 1
PMCID: PMC250225  PMID: 1920611

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Akusjärvi G., Mathews M. B., Andersson P., Vennström B., Pettersson U. Structure of genes for virus-associated RNAI and RNAII of adenovirus type 2. Proc Natl Acad Sci U S A. 1980 May;77(5):2424–2428. doi: 10.1073/pnas.77.5.2424. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bhat R. A., Thimmappaya B. Construction and analysis of additional adenovirus substitution mutants confirm the complementation of VAI RNA function by two small RNAs encoded by Epstein-Barr virus. J Virol. 1985 Dec;56(3):750–756. doi: 10.1128/jvi.56.3.750-756.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bhat R. A., Thimmappaya B. Two small RNAs encoded by Epstein-Barr virus can functionally substitute for the virus-associated RNAs in the lytic growth of adenovirus 5. Proc Natl Acad Sci U S A. 1983 Aug;80(15):4789–4793. doi: 10.1073/pnas.80.15.4789. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Clarke P. A., Schwemmle M., Schickinger J., Hilse K., Clemens M. J. Binding of Epstein-Barr virus small RNA EBER-1 to the double-stranded RNA-activated protein kinase DAI. Nucleic Acids Res. 1991 Jan 25;19(2):243–248. doi: 10.1093/nar/19.2.243. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Clarke P. A., Sharp N. A., Clemens M. J. Translational control by the Epstein-Barr virus small RNA EBER-1. Reversal of the double-stranded RNA-induced inhibition of protein synthesis in reticulocyte lysates. Eur J Biochem. 1990 Nov 13;193(3):635–641. doi: 10.1111/j.1432-1033.1990.tb19381.x. [DOI] [PubMed] [Google Scholar]
  6. Colthurst D. R., Campbell D. G., Proud C. G. Structure and regulation of eukaryotic initiation factor eIF-2. Sequence of the site in the alpha subunit phosphorylated by the haem-controlled repressor and by the double-stranded RNA-activated inhibitor. Eur J Biochem. 1987 Jul 15;166(2):357–363. doi: 10.1111/j.1432-1033.1987.tb13523.x. [DOI] [PubMed] [Google Scholar]
  7. Davies M. V., Furtado M., Hershey J. W., Thimmappaya B., Kaufman R. J. Complementation of adenovirus virus-associated RNA I gene deletion by expression of a mutant eukaryotic translation initiation factor. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9163–9167. doi: 10.1073/pnas.86.23.9163. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Duncan R., Hershey J. W. Identification and quantitation of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional polyacrylamide gel electrophoresis. J Biol Chem. 1983 Jun 10;258(11):7228–7235. [PubMed] [Google Scholar]
  9. Farrell P. J., Hunt T., Jackson R. J. Analysis of phosphorylation of protein synthesis initiation factor eIF-2 by two-dimensional gel electrophoresis. Eur J Biochem. 1978 Sep 1;89(2):517–521. doi: 10.1111/j.1432-1033.1978.tb12556.x. [DOI] [PubMed] [Google Scholar]
  10. Fowlkes D. M., Shenk T. Transcriptional control regions of the adenovirus VAI RNA gene. Cell. 1980 Nov;22(2 Pt 2):405–413. doi: 10.1016/0092-8674(80)90351-7. [DOI] [PubMed] [Google Scholar]
  11. Furtado M. R., Subramanian S., Bhat R. A., Fowlkes D. M., Safer B., Thimmappaya B. Functional dissection of adenovirus VAI RNA. J Virol. 1989 Aug;63(8):3423–3434. doi: 10.1128/jvi.63.8.3423-3434.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Galabru J., Katze M. G., Robert N., Hovanessian A. G. The binding of double-stranded RNA and adenovirus VAI RNA to the interferon-induced protein kinase. Eur J Biochem. 1989 Jan 2;178(3):581–589. doi: 10.1111/j.1432-1033.1989.tb14485.x. [DOI] [PubMed] [Google Scholar]
  13. Guilfoyle R., Weinmann R. Control region for adenovirus VA RNA transcription. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3378–3382. doi: 10.1073/pnas.78.6.3378. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Gunnery S., Rice A. P., Robertson H. D., Mathews M. B. Tat-responsive region RNA of human immunodeficiency virus 1 can prevent activation of the double-stranded-RNA-activated protein kinase. Proc Natl Acad Sci U S A. 1990 Nov;87(22):8687–8691. doi: 10.1073/pnas.87.22.8687. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Hayes B. W., Telling G. C., Myat M. M., Williams J. F., Flint S. J. The adenovirus L4 100-kilodalton protein is necessary for efficient translation of viral late mRNA species. J Virol. 1990 Jun;64(6):2732–2742. doi: 10.1128/jvi.64.6.2732-2742.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Hovanessian A. G. The double stranded RNA-activated protein kinase induced by interferon: dsRNA-PK. J Interferon Res. 1989 Dec;9(6):641–647. doi: 10.1089/jir.1989.9.641. [DOI] [PubMed] [Google Scholar]
  17. Howe J. G., Hershey J. W. Translational initiation factor and ribosome association with the cytoskeletal framework fraction from HeLa cells. Cell. 1984 May;37(1):85–93. doi: 10.1016/0092-8674(84)90303-9. [DOI] [PubMed] [Google Scholar]
  18. Huang J. T., Schneider R. J. Adenovirus inhibition of cellular protein synthesis involves inactivation of cap-binding protein. Cell. 1991 Apr 19;65(2):271–280. doi: 10.1016/0092-8674(91)90161-q. [DOI] [PubMed] [Google Scholar]
  19. Hunter T., Hunt T., Jackson R. J., Robertson H. D. The characteristics of inhibition of protein synthesis by double-stranded ribonucleic acid in reticulocyte lysates. J Biol Chem. 1975 Jan 25;250(2):409–417. [PubMed] [Google Scholar]
  20. Katze M. G., DeCorato D., Safer B., Galabru J., Hovanessian A. G. Adenovirus VAI RNA complexes with the 68 000 Mr protein kinase to regulate its autophosphorylation and activity. EMBO J. 1987 Mar;6(3):689–697. doi: 10.1002/j.1460-2075.1987.tb04809.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Kaufman R. J., Murtha P. Translational control mediated by eucaryotic initiation factor-2 is restricted to specific mRNAs in transfected cells. Mol Cell Biol. 1987 Apr;7(4):1568–1571. doi: 10.1128/mcb.7.4.1568. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Kitajewski J., Schneider R. J., Safer B., Munemitsu S. M., Samuel C. E., Thimmappaya B., Shenk T. Adenovirus VAI RNA antagonizes the antiviral action of interferon by preventing activation of the interferon-induced eIF-2 alpha kinase. Cell. 1986 Apr 25;45(2):195–200. doi: 10.1016/0092-8674(86)90383-1. [DOI] [PubMed] [Google Scholar]
  23. Kitajewski J., Schneider R. J., Safer B., Shenk T. An adenovirus mutant unable to express VAI RNA displays different growth responses and sensitivity to interferon in various host cell lines. Mol Cell Biol. 1986 Dec;6(12):4493–4498. doi: 10.1128/mcb.6.12.4493. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Kostura M., Mathews M. B. Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI. Mol Cell Biol. 1989 Apr;9(4):1576–1586. doi: 10.1128/mcb.9.4.1576. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Lenk R., Ransom L., Kaufmann Y., Penman S. A cytoskeletal structure with associated polyribosomes obtained from HeLa cells. Cell. 1977 Jan;10(1):67–78. doi: 10.1016/0092-8674(77)90141-6. [DOI] [PubMed] [Google Scholar]
  26. Lerner M. R., Boyle J. A., Hardin J. A., Steitz J. A. Two novel classes of small ribonucleoproteins detected by antibodies associated with lupus erythematosus. Science. 1981 Jan 23;211(4480):400–402. doi: 10.1126/science.6164096. [DOI] [PubMed] [Google Scholar]
  27. Leroux A., London I. M. Regulation of protein synthesis by phosphorylation of eukaryotic initiation factor 2 alpha in intact reticulocytes and reticulocyte lysates. Proc Natl Acad Sci U S A. 1982 Apr;79(7):2147–2151. doi: 10.1073/pnas.79.7.2147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Maran A., Mathews M. B. Characterization of the double-stranded RNA implicated in the inhibition of protein synthesis in cells infected with a mutant adenovirus defective for VA RNA. Virology. 1988 May;164(1):106–113. doi: 10.1016/0042-6822(88)90625-3. [DOI] [PubMed] [Google Scholar]
  29. Mathews M. B. Binding of adenovirus VA RNA to mRNA: a possible role in splicing? Nature. 1980 Jun 19;285(5766):575–577. doi: 10.1038/285575a0. [DOI] [PubMed] [Google Scholar]
  30. Mathews M. B., Francoeur A. M. La antigen recognizes and binds to the 3'-oligouridylate tail of a small RNA. Mol Cell Biol. 1984 Jun;4(6):1134–1140. doi: 10.1128/mcb.4.6.1134. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Mathews M. B. Genes for VA-RNA in adenovirus 2. Cell. 1975 Oct;6(2):223–229. doi: 10.1016/0092-8674(75)90013-6. [DOI] [PubMed] [Google Scholar]
  32. Mathews M. B., Pettersson U. The low molecular weight of RNAs of adenovirus 2-infected cells. J Mol Biol. 1978 Feb 25;119(2):293–328. doi: 10.1016/0022-2836(78)90439-4. [DOI] [PubMed] [Google Scholar]
  33. Mellits K. H., Kostura M., Mathews M. B. Interaction of adenovirus VA RNAl with the protein kinase DAI: nonequivalence of binding and function. Cell. 1990 Jun 1;61(5):843–852. doi: 10.1016/0092-8674(90)90194-j. [DOI] [PubMed] [Google Scholar]
  34. Mellits K. H., Mathews M. B. Effects of mutations in stem and loop regions on the structure and function of adenovirus VA RNAI. EMBO J. 1988 Sep;7(9):2849–2859. doi: 10.1002/j.1460-2075.1988.tb03141.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Meurs E., Chong K., Galabru J., Thomas N. S., Kerr I. M., Williams B. R., Hovanessian A. G. Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell. 1990 Jul 27;62(2):379–390. doi: 10.1016/0092-8674(90)90374-n. [DOI] [PubMed] [Google Scholar]
  36. Minks M. A., West D. K., Benvin S., Baglioni C. Structural requirements of double-stranded RNA for the activation of 2',5'-oligo(A) polymerase and protein kinase of interferon-treated HeLa cells. J Biol Chem. 1979 Oct 25;254(20):10180–10183. [PubMed] [Google Scholar]
  37. O'Malley R. P., Duncan R. F., Hershey J. W., Mathews M. B. Modification of protein synthesis initiation factors and the shut-off of host protein synthesis in adenovirus-infected cells. Virology. 1989 Jan;168(1):112–118. doi: 10.1016/0042-6822(89)90409-1. [DOI] [PubMed] [Google Scholar]
  38. O'Malley R. P., Mariano T. M., Siekierka J., Mathews M. B. A mechanism for the control of protein synthesis by adenovirus VA RNAI. Cell. 1986 Feb 14;44(3):391–400. doi: 10.1016/0092-8674(86)90460-5. [DOI] [PubMed] [Google Scholar]
  39. Pathak V. K., Schindler D., Hershey J. W. Generation of a mutant form of protein synthesis initiation factor eIF-2 lacking the site of phosphorylation by eIF-2 kinases. Mol Cell Biol. 1988 Feb;8(2):993–995. doi: 10.1128/mcb.8.2.993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Pettersson U., Philipson L. Location of sequences on the adenovirus genome coding for the 5.5S RNA. Cell. 1975 Sep;6(1):1–4. doi: 10.1016/0092-8674(75)90066-5. [DOI] [PubMed] [Google Scholar]
  41. Price R., Penman S. Transcription of the adenovirus genome by an -amanitine-sensitive ribonucleic acid polymerase in HeLa cells. J Virol. 1972 Apr;9(4):621–626. doi: 10.1128/jvi.9.4.621-626.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Reich P. R., Forget B. G., Weissman S. M. RNA of low molecular weight in KB cells infected with adenovirus type 2. J Mol Biol. 1966 Jun;17(2):428–439. doi: 10.1016/s0022-2836(66)80153-5. [DOI] [PubMed] [Google Scholar]
  43. Reichel P. A., Merrick W. C., Siekierka J., Mathews M. B. Regulation of a protein synthesis initiation factor by adenovirus virus-associated RNA. Nature. 1985 Jan 17;313(5999):196–200. doi: 10.1038/313196a0. [DOI] [PubMed] [Google Scholar]
  44. Rowlands A. G., Panniers R., Henshaw E. C. The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2. J Biol Chem. 1988 Apr 25;263(12):5526–5533. [PubMed] [Google Scholar]
  45. Roy S., Agy M., Hovanessian A. G., Sonenberg N., Katze M. G. The integrity of the stem structure of human immunodeficiency virus type 1 Tat-responsive sequence of RNA is required for interaction with the interferon-induced 68,000-Mr protein kinase. J Virol. 1991 Feb;65(2):632–640. doi: 10.1128/jvi.65.2.632-640.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Schneider R. J., Safer B., Munemitsu S. M., Samuel C. E., Shenk T. Adenovirus VAI RNA prevents phosphorylation of the eukaryotic initiation factor 2 alpha subunit subsequent to infection. Proc Natl Acad Sci U S A. 1985 Jul;82(13):4321–4325. doi: 10.1073/pnas.82.13.4321. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Schneider R. J., Weinberger C., Shenk T. Adenovirus VAI RNA facilitates the initiation of translation in virus-infected cells. Cell. 1984 May;37(1):291–298. doi: 10.1016/0092-8674(84)90325-8. [DOI] [PubMed] [Google Scholar]
  48. Siekierka J., Mariano T. M., Reichel P. A., Mathews M. B. Translational control by adenovirus: lack of virus-associated RNAI during adenovirus infection results in phosphorylation of initiation factor eIF-2 and inhibition of protein synthesis. Proc Natl Acad Sci U S A. 1985 Apr;82(7):1959–1963. doi: 10.1073/pnas.82.7.1959. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Strijker R., Fritz D. T., Levinson A. D. Adenovirus VAI-RNA regulates gene expression by controlling stability of ribosome-bound RNAs. EMBO J. 1989 Sep;8(9):2669–2675. doi: 10.1002/j.1460-2075.1989.tb08407.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Svensson C., Akusjärvi G. A novel effect of adenovirus VA RNA1 on cytoplasmic mRNA abundance. Virology. 1990 Feb;174(2):613–617. doi: 10.1016/0042-6822(90)90116-9. [DOI] [PubMed] [Google Scholar]
  51. Svensson C., Akusjärvi G. Adenovirus VA RNAI mediates a translational stimulation which is not restricted to the viral mRNAs. EMBO J. 1985 Apr;4(4):957–964. doi: 10.1002/j.1460-2075.1985.tb03724.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Svensson C., Akusjärvi G. Defective RNA splicing in the absence of adenovirus-associated RNAI. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4690–4694. doi: 10.1073/pnas.83.13.4690. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Swaminathan S., Tomkinson B., Kieff E. Recombinant Epstein-Barr virus with small RNA (EBER) genes deleted transforms lymphocytes and replicates in vitro. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1546–1550. doi: 10.1073/pnas.88.4.1546. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Söderlund H., Pettersson U., Vennström B., Philipson L., Mathews M. B. A new species of virus-coded low molecular weight RNA from cells infected with adenovirus type 2. Cell. 1976 Apr;7(4):585–593. doi: 10.1016/0092-8674(76)90209-9. [DOI] [PubMed] [Google Scholar]
  55. Thimmappaya B., Weinberger C., Schneider R. J., Shenk T. Adenovirus VAI RNA is required for efficient translation of viral mRNAs at late times after infection. Cell. 1982 Dec;31(3 Pt 2):543–551. doi: 10.1016/0092-8674(82)90310-5. [DOI] [PubMed] [Google Scholar]
  56. Weinmann R., Raskas H. J., Roeder R. G. Role of DNA-dependent RNA polymerases II and III in transcription of the adenovirus genome late in productive infection. Proc Natl Acad Sci U S A. 1974 Sep;71(9):3426–3439. doi: 10.1073/pnas.71.9.3426. [DOI] [PMC free article] [PubMed] [Google Scholar]
  57. Zain S., Gingeras T. R., Bullock P., Wong G., Gelinas R. E. Determination and analysis of adenovirus-2 DNA sequences which may include signals for late messenger RNA processing. J Mol Biol. 1979 Dec 5;135(2):413–433. doi: 10.1016/0022-2836(79)90444-3. [DOI] [PubMed] [Google Scholar]
  58. Zilberstein A., Federman P., Shulman L., Revel M. Specific phosphorylation in vitro of a protein associated with ribosomes of interferon-treated mouse L cells. FEBS Lett. 1976 Sep 15;68(1):119–124. doi: 10.1016/0014-5793(76)80418-8. [DOI] [PubMed] [Google Scholar]

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