C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids

RNA

Volumn 5, Issue 6, 1999, Pages 739-750

  Ebihara, Kanae ^a   Nakamura, Yoshikazu ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

EF Tu homology; eRF1; eRF3; G domain; Protein release factor; Sup35; Sup45; tRNA mimicry

Indexed keywords

AMINO ACID; AMPICILLIN; KANAMYCIN; TRANSLATION TERMINATION FACTOR;

ARTICLE; CARBOXY TERMINAL SEQUENCE; PLASMID; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; RNA TRANSLATION; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES POMBE; TRANSLATION REGULATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CONSERVED SEQUENCE; FUNGAL PROTEINS; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HUMANS; MOLECULAR SEQUENCE DATA; PEPTIDE TERMINATION FACTORS; PRIONS; PROTEIN BINDING; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SCHIZOSACCHAROMYCES; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0033016754     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1017/S135583829998216X     Document Type: Article

References (35)

1. Ævarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Yu, Al-Karadaghi S, Svensson LA, Liljas A. 1994. Three-dimensional structure of the ribosomal translocase: Elongation factor G from Thermus thermophilus. EMBO J 13:3669-3677.
2. Ahmadian MR, Kreutzer R, Blechschmidt B, Sprinzl M. 1995. Site-directed mutagenesis of Thermus thermophilus EF-Tu: The substitution of threonine-62 by serine or alanine. FEBS Lett 377: 253-257.
3. Chien C-T, Bartel PL, Sternglanz R, Fields S. 1991. The two-hybrid system: A method to identify and clone genes for promoters that interact with a protein of interest. Proc Natl Acad Sci USA 08:9578-9582.
4. Czaplinski K, Ruiz-Echevarria MJ, Paushkin SV, Han X, Weng Y, Perlick HA, Dietz HC, Ter-Avanesyan MD, Peltz SW. 1998. The surveillance complex interacts with the translation release factors to enhance termination and degrade aberrant mRNAs. Genes & Dev 12:1665-1677.
5. Czworkowski J, Wang J, Steitz TA, Moore PB. 1994. The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J 13:3661-3668.
6. Devereux J, Haeberili P, Smithies O. 1984. A comprehensive set of sequence analysis programs for the Vax. Nucleic Acids Res 12:387-395.
7. Feilotter HE, Hannon GJ, Ruddel CJ, Beach D. 1994. Construction of an improved host strain for two hybrid screening. Nucleic Acids Res 22:1502-1503.
8. Fields S, Song O. 1989. A novel genetic system to detect protein-protein interaction. Nature 340:245-246.
9. Frolova LY, Simonsen JL, Merkulova TI, Litvinov DY, Martensen PM, Rechinsky VO, Camonis JH, Kisselev LL, Justesen J. 1998. 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 236:36-44.
10. Hoshino S, Miyazawa H, Enomoto T, Hanaoka F, Kikuchi Y, Kikuchi A, Ui M. 1989. 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 3:3807-3814.
11. Ito K, Ebihara K, Nakamura Y. 1998a. The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast. RNA 4:958-972.
12. Ito K, Ebihara K, Uno M, Nakamura Y. 1996. Conserved motifs of prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis. Proc Natl Acad Sci USA 93:5443-5448.
13. Ito K, Uno M, Nakamura Y. 1998b. Single amino acid substitution in prokaryote polypeptide release factor 2 permits it to terminate translation at all three stop codons. Proc Natl Acad Sci USA 95:8165-8169.
14. Jonak J, Anborgh PH, Parmeggiani A. 1994. Histidine-118 of elongation factor Tu: Its role in aminoacyl-tRNA binding and regulation of the GTPase activity. FEBS Lett 343:94-98.
15. Kikuchi Y, Shimatake H, Kikuchi A. 1988. A yeast gene required for the G1-to-S transition encodes a protein containing an A-kinase target site and GTPase domain. EMBO J 7:1175-1182.
16. Knudsen CR, Clark BF. 1995. Site-directed mutagenesis of Arg58 and Asp86 of elongation factor Tu from Escherichia coli: Effects on the GTPase reaction and aminoacyl-tRNA binding. Protein Eng 8:1267-1273.
17. Knudsen CR, Kjaersgard IV, Wiborg O, Clark BF. 1995. Mutation of the conserved Gly94 and Gly126 in elongation factor Tu from Escherichia coli. Elucidation of their structural and functional roles. Eur J Biochem 228:176-183.
18. Laurberg M, Mansilla F, Clark BF, Knudsen CR. 1998. Investigation of functional aspects of the N-terminal region of elongation factor Tu from Escherichia coli using a protein engineering approach. J Biol Chem 273:4387-4391.
19. Lindquist S. 1997. Mad cows meet psi-chotic yeast: The expansion of the prion hypothesis. Cell 89:495-498.
20. Mansilla F, Knudsen CR, Laurberg M, Clark BF. 1997. Mutational analysis of Escherichia coli elongation factor Tu in search of a role for the N-terminal region. Protein Eng 10:927-934.
21. Merkulova TI, Frolova LY, Lazar M, Camonis J, Kisselev LL. 1999. C-terminal domains of human translation termination factors eRF1 and eRF3 mediate their in vivo interaction. FEBS Lett 443:41-47.
22. Nakamura Y, Ito K. 1998. How protein reads the stop codon and terminates translation. Genes Cells 3:265-278.
23. Nakamura Y, Ito K, Isaksson LA. 1996. Emerging understanding of translation termination. Cell 87:147-150.
24. Nissen P, Kjeldgaard M, Thirup S, Clark BFC, Nyborg J. 1996. The ternary complex of aminoacylated tRNA and EF-Tu-GTP. Recognition of a bond and a fold. Biochimie 78:921-933.
25. Phe, EF-Tu, and a GTP analog. Science 270:1464-1472.
26. Paushkin SV, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD. 1997. Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: Implications for prion-dependent regulation. Mol Cell Biol 17:2798-2805.
27. Pedersen GN, Rattenborg T, Knudsen CR, Clark BF. 1998. The role of Glu259 in Escherichia coli elongation factor Tu in ternary complex formation. Protein Eng 11:101-108.
28. Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning: A laboratory manual, second edition. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
29. Sherman F. 1991. Getting started with yeast. Methods Enzymol 194: 3-20.
30. Smith DB, Johnson KS. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40.
31. Stansfield I, Jones KM, Kushnirov VV, Dagkesamanskay AR, Poznyakovski AI, Paushkin SV, Nierras CR, Cox BS, Ter-Avanesyan MD, Tuite MF. 1995. The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J 14:4365-4373.
32. Stansfield I, Tuite M. 1994. Polypeptide chain termination in Saccharomyces cerevisiae. Curr Genet 25:385-395.
33. Tubulekas I, Hughes D. 1993. A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome. J Bacteriol 175:240-250.
34. Wiborg O, Andersen C, Knudsen CR, Clark BFC, Nyborg J. 1996. Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA. J Biol Chem 271:20406-20411.
35. Zhouravleva G, Frolova L, Le Goff X, Le Guellec R, Inge-Vechtomov S, Kisselev L, Philippe M. 1995. Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J 14:4065-4072.