Skip to main content
PMC home page
RNA logoLink to RNA
. 2000 May;6(5):730–743. doi: 10.1017/s1355838200992392

Mtt1 is a Upf1-like helicase that interacts with the translation termination factors and whose overexpression can modulate termination efficiency.

K Czaplinski 1, N Majlesi 1, T Banerjee 1, S W Peltz 1
PMCID: PMC1369953  PMID: 10836794

Abstract

Translation termination is the final step that completes the synthesis of a polypeptide. Premature translation termination by introduction of a nonsense mutation leads to the synthesis of a truncated protein. We report the identification and characterization of the product of the MTT1 gene, a helicase belonging to the Upfl-like family of helicases that is involved in modulating translation termination. MTT1 is homologous to UPF1, a factor previously shown to function in both mRNA turnover and translation termination. Overexpression of MTT1 induced a nonsense suppression phenotype in a wild-type yeast strain. Nonsense suppression is apparently not due to induction of [PSI+], even though cooverexpression of HSP104 alleviated the nonsense suppression phenotype observed in cells overexpressing MTT1, suggesting a more direct role of Hsp104p in the translation termination process. The MTT1 gene product was shown to interact with translation termination factors and is localized to polysomes. Taken together, these results indicate that at least two members of a family of RNA helicases modulate translation termination efficiency in cells.

Full Text

The Full Text of this article is available as a PDF (946.5 KB).

Selected References

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

  1. Alani E., Cao L., Kleckner N. A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains. Genetics. 1987 Aug;116(4):541–545. doi: 10.1534/genetics.112.541.test. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. All-Robyn J. A., Kelley-Geraghty D., Griffin E., Brown N., Liebman S. W. Isolation of omnipotent suppressors in an [eta+] yeast strain. Genetics. 1990 Mar;124(3):505–514. doi: 10.1093/genetics/124.3.505. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Altamura N., Groudinsky O., Dujardin G., Slonimski P. P. NAM7 nuclear gene encodes a novel member of a family of helicases with a Zn-ligand motif and is involved in mitochondrial functions in Saccharomyces cerevisiae. J Mol Biol. 1992 Apr 5;224(3):575–587. doi: 10.1016/0022-2836(92)90545-u. [DOI] [PubMed] [Google Scholar]
  4. Anderson J. S., Parker R. RNA turnover: the helicase story unwinds. Curr Biol. 1996 Jul 1;6(7):780–782. doi: 10.1016/s0960-9822(02)00593-6. [DOI] [PubMed] [Google Scholar]
  5. Applequist S. E., Selg M., Raman C., Jäck H. M. Cloning and characterization of HUPF1, a human homolog of the Saccharomyces cerevisiae nonsense mRNA-reducing UPF1 protein. Nucleic Acids Res. 1997 Feb 15;25(4):814–821. doi: 10.1093/nar/25.4.814. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Barton-Davis E. R., Cordier L., Shoturma D. I., Leland S. E., Sweeney H. L. Aminoglycoside antibiotics restore dystrophin function to skeletal muscles of mdx mice. J Clin Invest. 1999 Aug;104(4):375–381. doi: 10.1172/JCI7866. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Bean D. W., Kallam W. E., Jr, Matson S. W. Purification and characterization of a DNA helicase from Saccharomyces cerevisiae. J Biol Chem. 1993 Oct 15;268(29):21783–21790. [PubMed] [Google Scholar]
  8. Bean D. W., Matson S. W. Identification of the gene encoding scHelI, a DNA helicase from Saccharomyces cerevisiae. Yeast. 1997 Dec;13(15):1465–1475. doi: 10.1002/(SICI)1097-0061(199712)13:15<1465::AID-YEA193>3.0.CO;2-U. [DOI] [PubMed] [Google Scholar]
  9. Bedwell D. M., Kaenjak A., Benos D. J., Bebok Z., Bubien J. K., Hong J., Tousson A., Clancy J. P., Sorscher E. J. Suppression of a CFTR premature stop mutation in a bronchial epithelial cell line. Nat Med. 1997 Nov;3(11):1280–1284. doi: 10.1038/nm1197-1280. [DOI] [PubMed] [Google Scholar]
  10. Biswas E. E., Chen P. H., Biswas S. B. DNA helicase associated with DNA polymerase alpha: isolation by a modified immunoaffinity chromatography. Biochemistry. 1993 Dec 14;32(49):13393–13398. doi: 10.1021/bi00212a003. [DOI] [PubMed] [Google Scholar]
  11. Biswas E. E., Chen P. H., Leszyk J., Biswas S. B. Biochemical and genetic characterization of a replication protein A dependent DNA helicase from the yeast, Saccharomyces cerevisiae. Biochem Biophys Res Commun. 1995 Jan 26;206(3):850–856. doi: 10.1006/bbrc.1995.1121. [DOI] [PubMed] [Google Scholar]
  12. Biswas E. E., Fricke W. M., Chen P. H., Biswas S. B. Yeast DNA helicase A: cloning, expression, purification, and enzymatic characterization. Biochemistry. 1997 Oct 28;36(43):13277–13284. doi: 10.1021/bi971292s. [DOI] [PubMed] [Google Scholar]
  13. Biswas S. B., Chen P. H., Biswas E. E. Purification and characterization of DNA polymerase alpha-associated replication protein A-dependent yeast DNA helicase A. Biochemistry. 1997 Oct 28;36(43):13270–13276. doi: 10.1021/bi9712910. [DOI] [PubMed] [Google Scholar]
  14. Buckingham R. H., Grentzmann G., Kisselev L. Polypeptide chain release factors. Mol Microbiol. 1997 May;24(3):449–456. doi: 10.1046/j.1365-2958.1997.3711734.x. [DOI] [PubMed] [Google Scholar]
  15. Budd M. E., Campbell J. L. A yeast replicative helicase, Dna2 helicase, interacts with yeast FEN-1 nuclease in carrying out its essential function. Mol Cell Biol. 1997 Apr;17(4):2136–2142. doi: 10.1128/mcb.17.4.2136. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Budd M. E., Choe W. C., Campbell J. L. DNA2 encodes a DNA helicase essential for replication of eukaryotic chromosomes. J Biol Chem. 1995 Nov 10;270(45):26766–26769. doi: 10.1074/jbc.270.45.26766. [DOI] [PubMed] [Google Scholar]
  17. Chernoff Y. O., Lindquist S. L., Ono B., Inge-Vechtomov S. G., Liebman S. W. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science. 1995 May 12;268(5212):880–884. doi: 10.1126/science.7754373. [DOI] [PubMed] [Google Scholar]
  18. Cui Y., Dinman J. D., Peltz S. W. Mof4-1 is an allele of the UPF1/IFS2 gene which affects both mRNA turnover and -1 ribosomal frameshifting efficiency. EMBO J. 1996 Oct 15;15(20):5726–5736. doi: 10.1002/j.1460-2075.1996.tb00956.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Cui Y., Hagan K. W., Zhang S., Peltz S. W. Identification and characterization of genes that are required for the accelerated degradation of mRNAs containing a premature translational termination codon. Genes Dev. 1995 Feb 15;9(4):423–436. doi: 10.1101/gad.9.4.423. [DOI] [PubMed] [Google Scholar]
  20. Czaplinski K., Ruiz-Echevarria M. J., González C. I., Peltz S. W. Should we kill the messenger? The role of the surveillance complex in translation termination and mRNA turnover. Bioessays. 1999 Aug;21(8):685–696. doi: 10.1002/(SICI)1521-1878(199908)21:8<685::AID-BIES8>3.0.CO;2-4. [DOI] [PubMed] [Google Scholar]
  21. Czaplinski K., Ruiz-Echevarria M. J., Paushkin S. V., Han X., Weng Y., Perlick H. A., Dietz H. C., Ter-Avanesyan M. D., Peltz S. W. The surveillance complex interacts with the translation release factors to enhance termination and degrade aberrant mRNAs. Genes Dev. 1998 Jun 1;12(11):1665–1677. doi: 10.1101/gad.12.11.1665. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Czaplinski K., Weng Y., Hagan K. W., Peltz S. W. Purification and characterization of the Upf1 protein: a factor involved in translation and mRNA degradation. RNA. 1995 Aug;1(6):610–623. [PMC free article] [PubMed] [Google Scholar]
  23. DeMarini D. J., Winey M., Ursic D., Webb F., Culbertson M. R. SEN1, a positive effector of tRNA-splicing endonuclease in Saccharomyces cerevisiae. Mol Cell Biol. 1992 May;12(5):2154–2164. doi: 10.1128/mcb.12.5.2154. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Didichenko S. A., Ter-Avanesyan M. D., Smirnov V. N. Ribosome-bound EF-1 alpha-like protein of yeast Saccharomyces cerevisiae. Eur J Biochem. 1991 Jun 15;198(3):705–711. doi: 10.1111/j.1432-1033.1991.tb16070.x. [DOI] [PubMed] [Google Scholar]
  25. Doel S. M., McCready S. J., Nierras C. R., Cox B. S. The dominant PNM2- mutation which eliminates the psi factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics. 1994 Jul;137(3):659–670. doi: 10.1093/genetics/137.3.659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Eurwilaichitr L., Graves F. M., Stansfield I., Tuite M. F. The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae. Mol Microbiol. 1999 May;32(3):485–496. doi: 10.1046/j.1365-2958.1999.01346.x. [DOI] [PubMed] [Google Scholar]
  27. Frolova L. Y., Simonsen J. L., Merkulova T. I., Litvinov D. Y., Martensen P. M., Rechinsky V. O., Camonis J. H., Kisselev L. L., Justesen J. Functional expression of eukaryotic polypeptide chain release factors 1 and 3 by means of baculovirus/insect cells and complex formation between the factors. Eur J Biochem. 1998 Aug 15;256(1):36–44. doi: 10.1046/j.1432-1327.1998.2560036.x. [DOI] [PubMed] [Google Scholar]
  28. Frolova L., Le Goff X., Zhouravleva G., Davydova E., Philippe M., Kisselev L. Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome-dependent guanosine triphosphatase. RNA. 1996 Apr;2(4):334–341. [PMC free article] [PubMed] [Google Scholar]
  29. Glover J. R., Kowal A. S., Schirmer E. C., Patino M. M., Liu J. J., Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell. 1997 May 30;89(5):811–819. doi: 10.1016/s0092-8674(00)80264-0. [DOI] [PubMed] [Google Scholar]
  30. Glover J. R., Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell. 1998 Jul 10;94(1):73–82. doi: 10.1016/s0092-8674(00)81223-4. [DOI] [PubMed] [Google Scholar]
  31. Gorbalenya A. E., Koonin E. V., Donchenko A. P., Blinov V. M. A novel superfamily of nucleoside triphosphate-binding motif containing proteins which are probably involved in duplex unwinding in DNA and RNA replication and recombination. FEBS Lett. 1988 Aug 1;235(1-2):16–24. doi: 10.1016/0014-5793(88)81226-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Hagan K. W., Ruiz-Echevarria M. J., Quan Y., Peltz S. W. Characterization of cis-acting sequences and decay intermediates involved in nonsense-mediated mRNA turnover. Mol Cell Biol. 1995 Feb;15(2):809–823. doi: 10.1128/mcb.15.2.809. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. He F., Brown A. H., Jacobson A. Upf1p, Nmd2p, and Upf3p are interacting components of the yeast nonsense-mediated mRNA decay pathway. Mol Cell Biol. 1997 Mar;17(3):1580–1594. doi: 10.1128/mcb.17.3.1580. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. He F., Peltz S. W., Donahue J. L., Rosbash M., Jacobson A. Stabilization and ribosome association of unspliced pre-mRNAs in a yeast upf1- mutant. Proc Natl Acad Sci U S A. 1993 Aug 1;90(15):7034–7038. doi: 10.1073/pnas.90.15.7034. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Hentze M. W., Kulozik A. E. A perfect message: RNA surveillance and nonsense-mediated decay. Cell. 1999 Feb 5;96(3):307–310. doi: 10.1016/s0092-8674(00)80542-5. [DOI] [PubMed] [Google Scholar]
  36. Hilleren P., Parker R. mRNA surveillance in eukaryotes: kinetic proofreading of proper translation termination as assessed by mRNP domain organization? RNA. 1999 Jun;5(6):711–719. doi: 10.1017/s1355838299990519. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Hoshino S., Imai M., Mizutani M., Kikuchi Y., Hanaoka F., Ui M., Katada T. Molecular cloning of a novel member of the eukaryotic polypeptide chain-releasing factors (eRF). Its identification as eRF3 interacting with eRF1. J Biol Chem. 1998 Aug 28;273(35):22254–22259. doi: 10.1074/jbc.273.35.22254. [DOI] [PubMed] [Google Scholar]
  38. Hoshino S., Miyazawa H., Enomoto T., Hanaoka F., Kikuchi Y., Kikuchi A., Ui M. A human homologue of the yeast GST1 gene codes for a GTP-binding protein and is expressed in a proliferation-dependent manner in mammalian cells. EMBO J. 1989 Dec 1;8(12):3807–3814. doi: 10.1002/j.1460-2075.1989.tb08558.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Howard M., Frizzell R. A., Bedwell D. M. Aminoglycoside antibiotics restore CFTR function by overcoming premature stop mutations. Nat Med. 1996 Apr;2(4):467–469. doi: 10.1038/nm0496-467. [DOI] [PubMed] [Google Scholar]
  40. Ito K., Ebihara K., Nakamura Y. The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast. RNA. 1998 Aug;4(8):958–972. doi: 10.1017/s1355838298971874. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Kikuchi Y., Shimatake H., Kikuchi A. A yeast gene required for the G1-to-S transition encodes a protein containing an A-kinase target site and GTPase domain. EMBO J. 1988 Apr;7(4):1175–1182. doi: 10.1002/j.1460-2075.1988.tb02928.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Koonin E. V. A new group of putative RNA helicases. Trends Biochem Sci. 1992 Dec;17(12):495–497. doi: 10.1016/0968-0004(92)90338-a. [DOI] [PubMed] [Google Scholar]
  43. Korolev S., Hsieh J., Gauss G. H., Lohman T. M., Waksman G. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell. 1997 Aug 22;90(4):635–647. doi: 10.1016/s0092-8674(00)80525-5. [DOI] [PubMed] [Google Scholar]
  44. Korolev S., Yao N., Lohman T. M., Weber P. C., Waksman G. Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases. Protein Sci. 1998 Mar;7(3):605–610. doi: 10.1002/pro.5560070309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Le Goff X., Philippe M., Jean-Jean O. Overexpression of human release factor 1 alone has an antisuppressor effect in human cells. Mol Cell Biol. 1997 Jun;17(6):3164–3172. doi: 10.1128/mcb.17.6.3164. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Leeds P., Peltz S. W., Jacobson A., Culbertson M. R. The product of the yeast UPF1 gene is required for rapid turnover of mRNAs containing a premature translational termination codon. Genes Dev. 1991 Dec;5(12A):2303–2314. doi: 10.1101/gad.5.12a.2303. [DOI] [PubMed] [Google Scholar]
  47. Leeds P., Wood J. M., Lee B. S., Culbertson M. R. Gene products that promote mRNA turnover in Saccharomyces cerevisiae. Mol Cell Biol. 1992 May;12(5):2165–2177. doi: 10.1128/mcb.12.5.2165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Lussier M., White A. M., Sheraton J., di Paolo T., Treadwell J., Southard S. B., Horenstein C. I., Chen-Weiner J., Ram A. F., Kapteyn J. C. Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae. Genetics. 1997 Oct;147(2):435–450. doi: 10.1093/genetics/147.2.435. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Masison D. C., Maddelein M. L., Wickner R. B. The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation. Proc Natl Acad Sci U S A. 1997 Nov 11;94(23):12503–12508. doi: 10.1073/pnas.94.23.12503. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Nakamura Y., Ito K., Isaksson L. A. Emerging understanding of translation termination. Cell. 1996 Oct 18;87(2):147–150. doi: 10.1016/s0092-8674(00)81331-8. [DOI] [PubMed] [Google Scholar]
  51. Palmer E., Wilhelm J. M., Sherman F. Phenotypic suppression of nonsense mutants in yeast by aminoglycoside antibiotics. Nature. 1979 Jan 11;277(5692):148–150. doi: 10.1038/277148a0. [DOI] [PubMed] [Google Scholar]
  52. Patino M. M., Liu J. J., Glover J. R., Lindquist S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science. 1996 Aug 2;273(5275):622–626. doi: 10.1126/science.273.5275.622. [DOI] [PubMed] [Google Scholar]
  53. Paushkin S. V., Kushnirov V. V., Smirnov V. N., Ter-Avanesyan M. D. In vitro propagation of the prion-like state of yeast Sup35 protein. Science. 1997 Jul 18;277(5324):381–383. doi: 10.1126/science.277.5324.381. [DOI] [PubMed] [Google Scholar]
  54. Paushkin S. V., Kushnirov V. V., Smirnov V. N., Ter-Avanesyan M. D. Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation. Mol Cell Biol. 1997 May;17(5):2798–2805. doi: 10.1128/mcb.17.5.2798. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Paushkin S. V., Kushnirov V. V., Smirnov V. N., Ter-Avanesyan M. D. Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J. 1996 Jun 17;15(12):3127–3134. [PMC free article] [PubMed] [Google Scholar]
  56. Perlick H. A., Medghalchi S. M., Spencer F. A., Kendzior R. J., Jr, Dietz H. C. Mammalian orthologues of a yeast regulator of nonsense transcript stability. Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10928–10932. doi: 10.1073/pnas.93.20.10928. [DOI] [PMC free article] [PubMed] [Google Scholar]
  57. Rozen F., Edery I., Meerovitch K., Dever T. E., Merrick W. C., Sonenberg N. Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F. Mol Cell Biol. 1990 Mar;10(3):1134–1144. doi: 10.1128/mcb.10.3.1134. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Ruiz-Echevarria M. J., Czaplinski K., Peltz S. W. Making sense of nonsense in yeast. Trends Biochem Sci. 1996 Nov;21(11):433–438. doi: 10.1016/s0968-0004(96)10055-4. [DOI] [PubMed] [Google Scholar]
  59. Scheffner M., Knippers R., Stahl H. RNA unwinding activity of SV40 large T antigen. Cell. 1989 Jun 16;57(6):955–963. doi: 10.1016/0092-8674(89)90334-6. [DOI] [PubMed] [Google Scholar]
  60. Schena M., Yamamoto K. R. Mammalian glucocorticoid receptor derivatives enhance transcription in yeast. Science. 1988 Aug 19;241(4868):965–967. doi: 10.1126/science.3043665. [DOI] [PubMed] [Google Scholar]
  61. Schiestl R. H., Gietz R. D. High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr Genet. 1989 Dec;16(5-6):339–346. doi: 10.1007/BF00340712. [DOI] [PubMed] [Google Scholar]
  62. Singh A., Ursic D., Davies J. Phenotypic suppression and misreading Saccharomyces cerevisiae. Nature. 1979 Jan 11;277(5692):146–148. doi: 10.1038/277146a0. [DOI] [PubMed] [Google Scholar]
  63. Snay-Hodge C. A., Colot H. V., Goldstein A. L., Cole C. N. Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export. EMBO J. 1998 May 1;17(9):2663–2676. doi: 10.1093/emboj/17.9.2663. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Song H., Mugnier P., Das A. K., Webb H. M., Evans D. R., Tuite M. F., Hemmings B. A., Barford D. The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell. 2000 Feb 4;100(3):311–321. doi: 10.1016/s0092-8674(00)80667-4. [DOI] [PubMed] [Google Scholar]
  65. Song J. M., Liebman S. W. Allosuppressors that enhance the efficiency of omnipotent suppressors in Saccharomyces cerevisiae. Genetics. 1987 Mar;115(3):451–460. doi: 10.1093/genetics/115.3.451. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Song J. M., Picologlou S., Grant C. M., Firoozan M., Tuite M. F., Liebman S. Elongation factor EF-1 alpha gene dosage alters translational fidelity in Saccharomyces cerevisiae. Mol Cell Biol. 1989 Oct;9(10):4571–4575. doi: 10.1128/mcb.9.10.4571. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Staley J. P., Guthrie C. Mechanical devices of the spliceosome: motors, clocks, springs, and things. Cell. 1998 Feb 6;92(3):315–326. doi: 10.1016/s0092-8674(00)80925-3. [DOI] [PubMed] [Google Scholar]
  68. Stansfield I., Jones K. M., Kushnirov V. V., Dagkesamanskaya A. R., Poznyakovski A. I., Paushkin S. V., Nierras C. R., Cox B. S., Ter-Avanesyan M. D., Tuite M. F. The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J. 1995 Sep 1;14(17):4365–4373. doi: 10.1002/j.1460-2075.1995.tb00111.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Stansfield I., Tuite M. F. Polypeptide chain termination in Saccharomyces cerevisiae. Curr Genet. 1994 May;25(5):385–395. doi: 10.1007/BF00351776. [DOI] [PubMed] [Google Scholar]
  70. Subramanya H. S., Bird L. E., Brannigan J. A., Wigley D. B. Crystal structure of a DExx box DNA helicase. Nature. 1996 Nov 28;384(6607):379–383. doi: 10.1038/384379a0. [DOI] [PubMed] [Google Scholar]
  71. Sun X., Perlick H. A., Dietz H. C., Maquat L. E. A mutated human homologue to yeast Upf1 protein has a dominant-negative effect on the decay of nonsense-containing mRNAs in mammalian cells. Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):10009–10014. doi: 10.1073/pnas.95.17.10009. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Ter-Avanesyan M. D., Kushnirov V. V., Dagkesamanskaya A. R., Didichenko S. A., Chernoff Y. O., Inge-Vechtomov S. G., Smirnov V. N. Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol Microbiol. 1993 Mar;7(5):683–692. doi: 10.1111/j.1365-2958.1993.tb01159.x. [DOI] [PubMed] [Google Scholar]
  73. Tseng S. S., Weaver P. L., Liu Y., Hitomi M., Tartakoff A. M., Chang T. H. Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export. EMBO J. 1998 May 1;17(9):2651–2662. doi: 10.1093/emboj/17.9.2651. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Velankar S. S., Soultanas P., Dillingham M. S., Subramanya H. S., Wigley D. B. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell. 1999 Apr 2;97(1):75–84. doi: 10.1016/s0092-8674(00)80716-3. [DOI] [PubMed] [Google Scholar]
  75. Venema J., Bousquet-Antonelli C., Gelugne J. P., Caizergues-Ferrer M., Tollervey D. Rok1p is a putative RNA helicase required for rRNA processing. Mol Cell Biol. 1997 Jun;17(6):3398–3407. doi: 10.1128/mcb.17.6.3398. [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. Venema J., Tollervey D. Processing of pre-ribosomal RNA in Saccharomyces cerevisiae. Yeast. 1995 Dec;11(16):1629–1650. doi: 10.1002/yea.320111607. [DOI] [PubMed] [Google Scholar]
  77. Venkatesan M., Silver L. L., Nossal N. G. Bacteriophage T4 gene 41 protein, required for the synthesis of RNA primers, is also a DNA helicase. J Biol Chem. 1982 Oct 25;257(20):12426–12434. [PubMed] [Google Scholar]
  78. Vincent A., Newnam G., Liebman S. W. The yeast translational allosuppressor, SAL6: a new member of the PP1-like phosphatase family with a long serine-rich N-terminal extension. Genetics. 1994 Nov;138(3):597–608. doi: 10.1093/genetics/138.3.597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Wells D. R., Tanguay R. L., Le H., Gallie D. R. HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status. Genes Dev. 1998 Oct 15;12(20):3236–3251. doi: 10.1101/gad.12.20.3236. [DOI] [PMC free article] [PubMed] [Google Scholar]
  80. Weng Y., Czaplinski K., Peltz S. W. ATP is a cofactor of the Upf1 protein that modulates its translation termination and RNA binding activities. RNA. 1998 Feb;4(2):205–214. [PMC free article] [PubMed] [Google Scholar]
  81. Weng Y., Czaplinski K., Peltz S. W. Genetic and biochemical characterization of mutations in the ATPase and helicase regions of the Upf1 protein. Mol Cell Biol. 1996 Oct;16(10):5477–5490. doi: 10.1128/mcb.16.10.5477. [DOI] [PMC free article] [PubMed] [Google Scholar]
  82. Weng Y., Czaplinski K., Peltz S. W. Identification and characterization of mutations in the UPF1 gene that affect nonsense suppression and the formation of the Upf protein complex but not mRNA turnover. Mol Cell Biol. 1996 Oct;16(10):5491–5506. doi: 10.1128/mcb.16.10.5491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Wickner R. B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science. 1994 Apr 22;264(5158):566–569. doi: 10.1126/science.7909170. [DOI] [PubMed] [Google Scholar]
  84. Winey M., Culbertson M. R. Mutations affecting the tRNA-splicing endonuclease activity of Saccharomyces cerevisiae. Genetics. 1988 Apr;118(4):609–617. doi: 10.1093/genetics/118.4.609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Zhang S., Grosse F. Nuclear DNA helicase II unwinds both DNA and RNA. Biochemistry. 1994 Apr 5;33(13):3906–3912. doi: 10.1021/bi00179a016. [DOI] [PubMed] [Google Scholar]
  86. Zhouravleva G., Frolova L., Le Goff X., Le Guellec R., Inge-Vechtomov S., Kisselev L., Philippe M. Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J. 1995 Aug 15;14(16):4065–4072. doi: 10.1002/j.1460-2075.1995.tb00078.x. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from RNA are provided here courtesy of The RNA Society

RESOURCES