Initiation of protein synthesis in mammalian cells with codons other than AUG and amino acids other than methionine

Molecular and Cellular Biology

Volumn 18, Issue 9, 1998, Pages 5140-5147

  Drabkin, Harold J ^a   Rajbhandary, Uttam L ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

METHIONINE;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ANTICODON; ARTICLE; CONTROLLED STUDY; GENE MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN SYNTHESIS; REPORTER GENE; RNA TRANSLATION; SEQUENCE ANALYSIS; START CODON; STRUCTURE ACTIVITY RELATION; TRANSLATION INITIATION;

ANIMALIA; ESCHERICHIA COLI; EUKARYOTA; MAMMALIA;

EID: 0031842442     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.9.5140     Document Type: Article

References (60)

1. Arfin, S. T. M., R. L. Kendall, L. Hall, L. H. Weaver, A. E. Stewart, B. W. Matthews, and R. A. Bradshaw. 1995. Eukaryotic methionine-aminopeptidases: two classes of cobalt-dependent enzymes. Proc. Natl. Acad. Sci. USA 92:7714-7718.
2. Val gene family: organization, nucleotide sequence and homologous transcription of three single-copy genes. Gene 44:287-297.
3. Belgrader, P., J. Cheng, and L. E. Maquat. 1993. Evidence to implicate translation by ribosomes in the mechanism by which nonsense codons reduce the nuclear level of human triosephosphate isomerase mRNA. Proc. Natl. Acad. Sci USA 90:482-486.
4. Bjork, G. R. 1995. Biosynthesis and function of modified nucleosides, p. 165- 205. In D. Sol̈ and U. L. RajBhandary (ed.), tRNA: structure, biosynthesis, and function. American Society for Microbiology, Washington, D.C.
5. Brown, J. L. 1979. A comparison of the turnover of alpha-N-acetylated and nonacetylated mouse L-cell proteins. J. Biol. Chem. 254:1447-1479.
6. Chattapadhyay, R., H. Pelka, and L. H. Schulman. 1990. Initiation of in vivo protein synthesis with non-methionine amino acids. Biochemistry 29:4263- 4268.
7. met functions in directing the scanning ribosome to the start site of translation. Science 242: 93-97.
8. Descombes, P., and U. Schibier. 1991. A liver-enriched transcriptional activator protein, LAP, and a transcriptional inhibitory protein, LIP, are translated from the same mRNA. Cell 67:569-579.
9. Donahue, T. F., A. M. Cigan, E. K. Pabich, and B. C. Valavicius. 1988. Mutations at a Zn(II) finger motif in the yeast eIF-2β gene alter ribosomal start-site selection during the scanning process. Cell 54:621-632.
10. Drabkin, H. J., M. Estrella, and U. L. RajBhandary. 1998. Initiator-elongator discrimination in vertebrate tRNAs for protein synthesis. Mol. Cell. Biol. 18:1459-1466.
11. Drabkin, H. J., H.-J. Park, and U. L. RajBhandary. 1996. Amber suppression in mammalian cells dependent upon expression of an Escherichia coli aminoacyl-tRNA synthetase. Mol. Cell. Biol. 16:907-913.
12. Drabkin, H. J., and U. L. RajBhandary. 1985. Expression in vivo of a mutant human initiator methionine tRNA gene in mammalian cells using an SV40 vector. J. Biol. Chem. 260:5588-5545.
13. Fütterer J., Z. Kiss-Laszlo, and T. Hohn. 1993. Nonlinear ribosome migration on cauliflower mosaic virus 35S RNA. Cell 73:789-802.
14. Geballe, A. P. 1996. Translational control mediated by upstream AUG co- dons, p. 173-197. In J. W. B. Hershey. M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
15. Gillum, A., B. Roe, M. P. J. S. Anandraj, and U. L. RajBhandary. 1975. Nucleotide sequence of human placenta cytoplasmic initiator tRNA. Cell 6: 407-113.
16. Hann, S. R., K. Sloan-Brown, and G. D. Spotts. 1992. Translational activation of the non-AUG-initiated c-myc 1 protein at high cell densities due to methionine deprivation. Genes Dev. 6:1229-1240.
17. Hinnebusch, A. G. 1997. Translation regulation of yeast GCN4, J. Biol. Chem. 272:21661-21664.
18. Ho, Y.-S., and Y. W. Kan. 1987. In vivo aminoacylation of human and Xenopus suppressor tRNAs constructed by site-specific mutagenesis. Proc. Natl. Acad. Sci. USA 84:2185-2188.
19. Huang. H. K., H. Yoon, E. M. Hannig, and T. F. Donahue. 1997. GTP hydrolysis controls stringent selection of the AUG start codon during Iranslation initiation in Saccharomyces cerevisiae. Genes Dev. 11:2396-2413.
20. Jackson, R. T. 1996. A comparative view of initiation site selection mechanisms, p. 71-112. In J. W. B. Hershey, M. B. Matthews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
21. Jang, S. K., M. V. Davits, R. J. Kaufman, and E. Wimmer. 1989. Initiation of protein synthesis by internal entry of ribosomes into the 5′ nontranslated region of encephalomyocarditis virus RNA in vivo. J. Virol. 63:651-1660.
22. Kendall, R. L., and R. A. Bradshaw. 1992. Isolation and characterization of the methionine aminopeptidase from porcine liver responsible for the cotranslational processing of proteins. J. Biol. Chem. 267:20667-20673.
23. Kluxen, F.-W., and H. Lubbert. 1993. Maximal expression of recombinant cDNAs in COS cells for use in expression cloning. Anal. Biochem. 208:352- 356.
24. Kozak, M. 1983. Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol. Rev. 47:1-455.
25. Kozak, M. 1992. Regulation of translation in eukaryotic systems. Annu. Rev. Cell Biol. 8:197-225.
26. Kozak, M. 1997. Recognition of AUG and alternative initiator codons is augmented by G in position +4 but is not generally affected by the nucleotides in positions +5 and +6. EMBO J. 16:2482-2492.
27. Li, S., N. V. Kumar, U. Varshney, and U. L. RajBhandary. 1996. Important role of the amino acid attached to tRNA in formylation and in initiation of protein synthesis in Escherichia coli. J. Biol. Chem. 271:1022-1028.
28. Liu, Y., N. Y. Garceau, J. J. Loros, and J. C. Dunlap. 1997. Thermally regulated translational control of FRQ mediates aspects of temperature responses in the Neurospora circadian clock. Cell 89:47-486.
29. Macejak, D. G., and P. Sarnow. 1991. Internal initiation of translation mediated by the 5′ leader of a cellular mRNA. Nature 353:90-94.
30. Mangroo, D., P. A. Limbach, J. A. McCloskey, and U. L. RajBhandary. 1995. An anticodon sequence mutant of Escherichia coli initiator tRNA: possible importance of a newly acquired base modification next to the anticodon on its activity in initiation. J. Bacteriol. 177:2858-2862.
31. Matthaei, J. H., H. P. Voigt, G. Heller, R. Neth, G. Schöch, H. Kübier, F. Amaelunxeu, G. Sander, and A. Parmeggiani. 1966. Specific interactions of ribosomes in decoding. Cold Spring Harbor Symp. Quant. Biol. 31:25-38.
32. Matthews, M. B. 1996. Interactions between viruses and the cellular machinery for protein synthesis, p. 505-548. In J. W. B. Hershey, M. B. Matthews and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
33. McDonald, J. K., and A. J. Barrett. 1986. Mammalian proteases, a glossary and bibliography, vol. 2. Exopeptidases. Academic Press, New York, N.Y.
34. Mellor, A., and A. E. Smith. 1978. Characterization of the amino-terminal tryptic peptide of simian virus 40 small-t and large-T antigens. J. Virol. 28: 992-996.
35. Moerschell, R. P., Y. Hosokawa, S. Tsunasawa, and F. Sherman. 1990. The specificities of yeast methionine aminopeptidase and acetylation of amino- terminal methionine in vivo. Processing of altered iso-1-cytochromes C created by oligonucleotide transformation. J. Biol. Chem. 265:19638-19643.
36. Pak, M., L. Pallanck, and L. H. Schulman. 1992. Conversion of a methionine initiator tRNA into a tryptophan-inserting tRNA in vivo. Biochemistry 31: 3303-3309.
37. Pallanck, L., and L. H. Schulman. 1991. Anticodon-dependent aminoacylation of a noncognate tRNA with isoleucine, valine, and phenylalanine in vivo. Proc. Natl. Acad. Sci. USA 88:3872-3876.
38. Pallanck, L., S. Li, and L. H. Shulman. 1992. The anticodon and discriminator base are major determinants of cysteine tRNA in vivo. J. Biol. Chem. 267:7221-7223.
39. Peabody, D. S. 1989. Translation initiation at non-AUG triplets in mammalian cells. J. Biol. Chem. 264:5031-5035.
40. Pelletier, J., and N. Sonenberg. 1988. Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from polio virus RNA. Nature 324:320-325.
41. Peltz, S. W., A. H. Brown, and A. Jacobson. 1993. mRNA destabilization triggered by premature translational termination depends on at least three cis-acting sequence elements and one trans-acting factor. Genes Dev. 7: 1737-1754.
42. RajBhandary, U. L. 1994. Initiator transfer RNAs. J. Bacteriol. 176:547-552.
43. RajBhandary, U. L., and C. M. Chow. 1995. Initiator tRNAs and initiation of protein synthesis, p. 511-528. In D. Söll and U. L. RajBhandary (ed.), tRNA: structure, biosynthesis, and function. ASM Press, Washington, D.C.
44. Reddy, H., B. Thimmappaya, R. Dhar, K. N. Subramanian, B. S. Zain, J. Pan, P. K. Ghosh, M. L. Celma, and S. M. Weissman. 1978. The genome of SV40. Science 200:494-502.
45. Sayers, J. R., W. Schmidt, and F. Eckstein. 1988. 5′-3′ exonuclease in phosphorothioate-based oligonucleotide-directed mutagenesis. Nucleic Acids Res. 16:791-802.
46. Schulman, L. H., and H. Pelka. 1985. In vitro conversion of a methionine to a glutamine-acceptor tRNA. Biochemistry 24:7309-7314.
47. Seong, B. L., C. P. Lee, and U. L. RajBhandary. 1989. Suppression of amber codons in vivo as evidence that mutants derived from E. coli initiator tRNA can act at the step of elongation in protein synthesis. J. Biol. Chem. 246: 6504-6508.
48. Shaw, W. V. 1975. Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria. Methods Enzymol. 43:737-755.
49. Stewart, J. W., F. Sherman, N. A. Shipman, and M. Jackson. 1971. Identification and mutational relocation of the AUG codon initiating translation of iso-1-cytochrome c in yeast. J. Biol. Chem. 246:7429-7445.
50. Varshney, U., C. P. Lee, and U. L. RajBhandary. 1991. Direct analysis of aminoacylation levels of tRNAs in vivo. J. Biol. Chem. 266:24712-24718.
51. Varshney, U., C. P. Lee, and U. L. RajBhandary. 1993. From elongator tRNA to initiator tRNA. Proc. Natl. Acad. Sci. USA 90:2305-2309.
52. Varshney, U., C.-P. Lee, B. L. Seong, and U. L. RajBhandary. 1991. Mutants of initiator tRNA that function both as initiators and elongators. J. Biol. Chem. 266:18018-18024.
53. Varshney, U., and U. L. RajBhandary. 1990. Initiation of protein synthesis from a termination codon. Proc. Natl. Acad. Sci. USA 87:1586-1590.
54. Varshney, U., and U. L. RajBhandary. 1992. Role of methionine and formylation of initiator tRNA in initiation of protein synthesis in Escherichia coli. J. Bacteriol. 174:7819-7826.
55. Wagner, T., M. Gross, and P. B. Sigler. 1984. Isoleucyl initiator tRNA does not initiate eucaryotic protein synthesis. J. Biol. Chem. 259:4706-4709.
56. Wu, X.-Q., P. Iyengar, and U. L. RajBhandary. 1996. Ribosome-initiator tRNA complex as an intermediate in translation initiation in Escherichia coli revealed by use of mutant initiator tRNAs and specialized ribosomes. EMBO J. 15:734-739.
57. Wu, X.-Q., and U. L. RajBhandary. 1997. Effect of the amino acid attached to Escherichia coli initiator tRNA on its affinity for the initiation factor IF2 and on the IF2 dependence of its binding to the ribosome. J. Biol. Chem. 272:1891-1895.
58. Yamao, F. H., H. Inokuchi, H. Ozeki, and D. Söll. Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene. J. Biol. Chem. 257:11639-11643.
59. Zaidenzaig, Y., and W. V. Shaw. 1976. Affinity and hydrophobic chromatography of three variants of chloramphenicol acetyltransferases specified by R factors in Escherichia coli. FEBS Lett. 62:266-270.
60. Zhang, J., and L. E. Maquat. 1997. Evidence that translation reinitiation abrogates nonsense-mediated mRNA decay in mammalian cells. EMBO J. 16:826-833.