HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status

Genes and Development

Volumn 12, Issue 20, 1998, Pages 3236-3251

  Wells, Douglas R ^a   Tanguay, Robert L ^a,b   Le, Hanh ^a   Gallie, Daniel R ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

HSP101; Protein synthesis; RNA binding protein; Translation initiation

Indexed keywords

COMPLEMENTARY DNA; HEAT SHOCK PROTEIN; MESSENGER RNA; RNA BINDING PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; GENE MUTATION; GENETIC TRANSCRIPTION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN PURIFICATION; RNA BINDING; RNA SYNTHESIS; TRANSCRIPTION REGULATION; YEAST;

EUKARYOTA; NICOTIANA TABACUM;

EID: 0032532127     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.12.20.3236     Document Type: Article

References (45)

1. Altmann, M., N. Sonenberg, and H. Trachsel. 1989. Translation in Saccharomyces cerevisiae: Initiation factor 4E-dependent cell-free system. Mol. Cell. Biol. 9: 4467-4472.
2. Altmann, M., S. Blum, J. Pelletier, N. Sonenherg, T.M.A. Wilson, and H. Trachsel. 1990a. Translation initiation factor-dependent extracts from Saccharomyces cerevisiae. Biochim. Biophys. Acta 1050: 155-159.
3. Altmann, M., S. Blum, T.M.A. Wilson, and H. Trachsel. 1990b. The 5′-leader sequence of tobacco mosaic virus RNA mediates initiation-factor-4E-independent, but still initiation-factor-4A-independent translation in yeast extracts. Gene 91: 127-129.
4. Altmann, M., N. Schmitz, C. Berset, and H. Trachsel. 1997. A novel inhibitor of cap-dependent translation initiation in yeast: p20 competes with eIF4G for binding to eIF4E. EMBO J. 16: 1114-1121.
5. Carrington, J.C. and D.D. Freed. 1990. Cap-independent enhancement of translation by a plant potyvirus 5′ nontranslated region. J. Virol. 64: 1590-1597.
6. Coppolecchia, R., P. Buser, A. Stotz, and P. Linder. 1993. A new yeast translation initiation factor suppresses a mutation in the eIF-4A RNA helicase. EMBO J. 12: 4005-4011.
7. Craig, A.W.B., A. Haghighat, A.T.K. Yu, and N. Sonenberg, 1998. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature 392: 520-523.
8. de la Cruz, J., I. Iost, D. Kressler, and P. Linder. 1997. The p20 and Ded1 proteins have antagonistic roles in eIF4E-dependent translation in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. 94: 5201-5206.
9. Dever, T.E., L. Feng, R.C. Wek, A.M. Cigan, T.F. Donahue, and A.G. Hinnebusch. 1992. Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 68: 585-596.
10. Ehrenfeld, E. 1996. Initiation of translation by picornavirus RNAs. In Translational control. (ed. M.B. Mathews, N. Sonenberg, and I.W.B. Hershey), pp. 549-574. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
11. Everett, J.G. and D.R. Gallie. 1992. RNA Delivery in Saccharomyces cerevisiae using electroporation. Yeast 8: 1007-1014.
12. Gallie, D.R. and V. Walbot. 1990. RNA pseudoknot domain of tobacco mosaic virus can functionally substitute for a poly(A) tail in plant and animal cells. Genes & Dev. 4: 1149-1157.
13. _. 1992. Identification of the motifs within the tobacco mosaic virus 5′-leader responsible for enhancing translation. Nucleic Acids Res. 20: 4631-4638.
14. Gallie, D.R., D.E. Sleat, J.W. Watts, P.C. Turner, and T.M.A. Wilson. 1987a. The 5′-leader sequence of tobacco mosaic virus RNA enhances the expression of foreign gene transcripts in vitro and in vivo. Nucleic Acids Res. 15: 3257-3273.
15. _. 1987b. A comparison of eukaryotic viral 5′-leader sequences as enhancers of mRNA expression in vivo. Nucleic Acids Res. 15: 8693-8711.
16. Gallie, D.R., W.J. Lucas, and V. Walbot. 1989. Visualizing mRNA expression in plant protoplasts: Factors influencing efficient mRNA uptake and translation. Plant Cell 1: 301-311.
17. Gallie, D.R., R.L. Tanguay, and V. Leathers. 1995. The tobacco etch viral 5′ leader and poly(A) tail are synergistic regulators of translation. Gene 165: 233-238.
18. Gietz, D., A. St. Jean, R.A. Woods, and R.H. Schiestl. 1992. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20: 1425.
19. Glover, J.R. and S. Lindquist. 1998. Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins. Cell 94: 73-82.
20. Goyer, C., M. Altmann, H.S. Lee, A. Blanc, M. Deshmukh, J.L. Woolford, H. Trachsel, and N. Sonenberg. 1993. TIF4631 and TIF4632: Two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function. Mol. Cell. Biol. 13: 4860-4874.
21. Hanic-Joyce, P.J., G.C. Johnston, and R.A. Singer. 1987. Regulated arrest of cell proliferation mediated by yeast prt1 mutations. Exp. Cell Res. 172: 134-145.
22. Hill, J., K.A. Donald, and D.E. Griffiths. 1991. DMSO-enhanced whole cell yeast transformation. Nucleic Acids Res. 19: 5791.
23. Hinnebusch, A.G. 1996. Translational control of GCN4: Gene-specific regulation by phosphorylation of eIF2. In Translational control (ed. M.B. Mathews, N. Sonenberg, and J.W.B. Hershey), pp. 199-244. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
24. Kozak, M. 1988. Leader length and secondary structure modulate mRNA function under conditions of stress. Mol. Cell. Biol. 8: 2737-2744.
25. _. 1991. An analysis of vertebrate mRNA sequences: Intimations of translational control. J. Cell. Biol. 115: 887-903.
26. _. 1992. A consideration of alternative models for the initiation of translation in eukaryotes. Crit. Rec. Biochem. Mol. Biol. 27: 385-402.
27. _. 1994. Determinants of translational fidelity and efficiency in vertebrate mRNAs. Biochimie 76: 815-821.
28. Lamphear, B.J., R. Kirchweger, T. Skern, and R.E. Rhoads. 1995. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. J. Biol. Chem. 270: 21975-21983.
29. Le, H., R.L. Tanguay, M.L. Balasta, C.-C. Wei, K.S. Browning, A.M. Metz, D.J. Goss, and D.R. Gallie. 1997. Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity. J. Biol. Chem. 272: 16247-16255.
30. Leathers, V., R. Tanguay, M. Kobayashi, and D.R. Gallie. 1993. A phylogenetically conserved sequence within viral 3′ untranslated RNA pseudoknots regulates translation. Mol. Cell. Biol. 13: 5331-5347.
31. Lee, Y.-R.J., R.T. Nagao, and J.L. Key. 1994. A soybean 101-kD heat shock protein complements a yeast HSP104 deletion mutant in acquiring thermotolerance. Plant Cell 6: 1889-1897.
32. Linder, P. and P.P. Slonimski. 1989. An essential yeast protein, encoded by duplicated genes TIF1 and TIF2 and homologous to the mammalian translation initiation factor eIF-4A, can suppress a mitochondrial missence mutation. Proc. Natl. Acad. Sci. 86: 2286-2290.
33. Merrick, W.C. and J.W.B. Hershey. 1996. In Translational control (ed. M.B. Mathews, N. Sonenberg, and J.W.B. Hershey), p. 31. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
34. Naranda, T., S.E. MacMillan, and J.W.B. Hershey. 1994. Purified yeast translational initiation factor eIF-3 is an RNA-binding protein complex that contains the PRT1 protein. J. Biol. Chem. 269: 32286-32292.
35. Parsell, D.A., Y. Sanchez, J.D. Stitzel, and S. Lindquist. 1991. Hsp104 is a highly conserved protein with two essential nucleotide-binding sites. Nature 353: 270-273.
36. Pelletier, J. and N. Sonenberg. 1985. Insertion mutagenesis to increase secondary structure within the 5′ noncoding region of a eukaryotic mRNA reduces translational efficiency. Cell 40: 515-526.
37. Phan, L., X. Zhang, K. Asano, J. Anderson, H.-P. Vornlochcr, J.R. Greenberg, J. Qin, and A.G. Hinnebusch. 1998. Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals that interacts with eIF5. Mol. Cell. Biol. 18: 4935-4946.
38. Rouault, T.A., R.D. Klausner, and J.E. Harford. 1996. Translational control of ferritin. In Translational control (ed. M.B. Mathews, N. Sonenberg, and J.W.B. Hershey), pp. 335-362. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
39. Sanchez, Y. and S. Lindquist. 1990. HSP104 required for induced thermotolerance. Science 248: 1112-1115.
40. Schirmer, E.C., S. Lindquist, and E. Vierling. 1994. An arabidopsis heat shock protein complements a thermotolerance defect in yeast. Plant Cell 6: 1899-1909.
41. Schmid, S.R. and P. Linder. 1991. Translation initiation factor 4A from Saccharomyces cerevisiae: Analysis of residues conserved in the D-E-A-D family of RNA helicases. Mol. Cell. Biol. 11: 3463-3471.
42. Sleat, D.E., R, Hull, P.C. Turner, and T.M.A. Wilson. 1988. Studies on the mechanism of translational enhancement by the 5′-leader sequence of tobacco mosaic virus RNA. Eur. J. Biochem. 175: 75-86.
43. Tanguay, R.L. and D.R. Gallie. 1996. Isolation and characterization of the 102-kilodalton RNA-binding protein that binds to the 5′ and 3′ translational enhancers of tobacco mosaic virus RNA. J. Biol. Chem. 271: 14316-14322.
44. Tarun, S.Z., S.E. Wells, J.A. Deardorff, and A.B. Sachs. 1997. Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation. Proc. Natl. Acad. Sci. 94: 9046-9051.
45. Van den Heuval, J.J. and H.A. Raue. 1992. Translational efficiency of mRNA in yeast cells is not increased by plant viral leader sequences. Appl. Microbiol. Biotechnol. 37: 84-87.