The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast

RNA

Volumn 4, Issue 8, 1998, Pages 958-972

  Ito, Koichi ^a   Ebihara, Kanae ^a   Nakamura, Yoshikazu ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

eRF1; eRF3; Protein release factor; Sup35; Sup45; Translation termination; tRNA mimicry

Indexed keywords

TRANSLATION TERMINATION FACTOR;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; MOLECULAR MIMICRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN SYNTHESIS; RNA STRUCTURE; RNA TRANSLATION; SACCHAROMYCES CEREVISIAE; TRANSLATION REGULATION;

AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; BINDING, COMPETITIVE; CLONING, MOLECULAR; DNA MUTATIONAL ANALYSIS; GENES, FUNGAL; GENETIC COMPLEMENTATION TEST; MODELS, MOLECULAR; MOLECULAR MIMICRY; MOLECULAR SEQUENCE DATA; PEPTIDE CHAIN TERMINATION, TRANSLATIONAL; PEPTIDE ELONGATION FACTOR TU; PEPTIDE FRAGMENTS; PEPTIDE TERMINATION FACTORS; PROTEIN BINDING; RNA, TRANSFER; SCHIZOSACCHAROMYCES; SEQUENCE ANALYSIS, DNA; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID;

EUKARYOTA; SACCHAROMYCES CEREVISIAE; SACCHAROMYCETALES; SCHIZOSACCHAROMYCES POMBE;

EID: 0031857784     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1355838298971874     Document Type: Article

References (39)

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. Bartel PL, Chien CT, Sternglanz R, Fields S. 1993a. Using the two-hybrid system to detect protein-protein interactions. In: Hartley DA, ed. Cellular interactions in development: A practical approach. Oxford: IRL Press at Oxford University Press, pp 153-179.
3. Bartel PL, Chien CT, Sternglanz R, Fields S. 1993b. Elimination of false positives that arise in using the two-hybrid system. Bio Technique 14:920-924.
4. Becker DM, Guarente L. 1991. High-efficiency transformation of yeast by electroporation. Methods Enzymol 194:182-186.
5. Breeden L, Nasmyth K. 1985. Regulation of the yeast HO gene. Cold Spring Harbor Symp Quant Biol 50:643-650.
6. Buckingham RH, Grentzmann G, Kisselev L. 1997. Polypeptide chain release factors. Mol Microbiol 24:449-456.
7. Chien CT, 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 88:9578-9582.
8. 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.
9. Devereux J, Haeberili P, Smithies O. 1984. A comprehensive set of sequence analysis programs for the Vax. Nucleic Acids Res 12:387-395.
10. 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.
11. Fields S, Song O. 1989. A novel genetic system to detect protein-protein interaction. Nature 340:245-246.
12. Finkelstein DB, Strausberg S. 1983. Heat shock-regulated production of Escherichia coli beta-galactosidase in Saccharomyces cerevisiae. Mol Cell Biol 3:1625-1633.
13. Frohman MA, Dush MK, Martin GR. 1988. Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer. Proc Natl Acad Sci USA 85:8998-9002.
14. Goff XL, Philippe M, Jean-Jean O. 1997. Overexpression of human release factor 1 alone has an antisuppressor effect in human cells. Mol Cell Biol 17:3164-3172.
15. 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.
16. Kawazu Y, Ito K, Matsumura K, Nakamura Y. 1995. Comparative characterization of release factor RF-3 genes of Escherichia coli, Salmonella typhimurium and Dichelobacter nodosus. J Bacteriol 177:5547-5553.
17. 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.
18. Lindquist S. 1997. Mad cows meet psi-chotic yeast: The expansion of the prion hypothesis. Cell 89:495-498.
19. Matsumura K, Ito K, Kawazu Y, Mikuni O, Nakamura Y. 1996. Suppression of temperature-sensitive defects of polypeptide release factors RF-1 and RF-2 by mutations or by an excess of RF-3 in Escherichia coli. J Mol Biol 250:588-599.
20. Mikuni O, Ito K, Moffat J, Matsumura K, McCaughan K, Nobukuni T, Tate W, Nakamura Y. 1994. Identification of the prfC gene, which encodes peptide-chain-release factor 3 of Escherichia coli. Proc Natl Acad Sci USA 91:5798-5802.
21. Miller J. 1972. Experiments in molecular genetics. Cold Spring Harbor: Cold Spring Harbor Laboratory Press.
22. Nakamura Y, Ito K, Isaksson LA. 1996. Emerging understanding of translation termination. Cell 87:147-150.
23. Nakamura Y, Ito K, Matsumura K, Kawazu Y, Ebihara K. 1995. Regulation of translation termination: Seven conserved domains for bacterial and eukaryotic polypeptide release factors. Biochem Cell Biol 73:1113-1122.
24. Phe, EF-Tu, and a GTP analog. Science 270: 1464-1472.
25. 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.
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. Saiki RK, Gelfand DH, Stoffel S, Scharf SJ, Higuchi R, Horn GT, Mullis KB, Erlich HA. 1988. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science 239: 487-491.
28. Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning: A laboratory manual, 2nd ed. Cold Spring Harbor: Cold Spring Harbor Laboratory Press.
29. Sanger F, Nicklen S, Coulson AR. 1977. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74:5463-5467.
30. Schiestl RH, Gietz RD. 1989. High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr Genetic 16:339-346.
31. Sherman F. 1991. Getting started with yeast. Methods Enzymol 194: 3-20.
32. Smith DB, Johnson KS. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40.
33. 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.
34. Stansfield I, Tuite M. 1994. Polypeptide chain termination in Saccharomyces cerevisiae. Curr Genet 25:385-395.
35. Tate WP, Brown CM. 1992. Translational termination: "Stop" for protein synthesis or "pause" for regulation of gene expression. Biochemistry 31:2443-2450.
36. Tuite M, Akhmaloka, Firoozan M, Duarte JAB, Grant CM. 1991. Control of translational accuracy in yeast: The role of the SAL4 (SUP45) protein. In: McCarthy J, Tuite M, eds. Post-transcriptional control of gene expression. Berlin/Heidelberg/New York: Springer Press, pp 611-622.
37. Vieira J, Messing J. 1987. Production of single-stranded plasmid DNA. Methods Enzymol 153:3-11.
38. Weiss RB, Murphy JP, Gallant JA. 1984. Genetic screen for cloned release factor genes. J Bacteriol 158:362-364.
39. 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.