Omnipotent role of archaeal elongation factor 1 alpha (EF1α) in translational elongation and termination, and quality control of protein synthesis

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 45, 2010, Pages 19242-19247

  Saitoa, Kazuki ^a   Kobayashi, Kan ^b   Wada, Miki ^a   Kikuno, Izumi ^b   Takusagawa, Akira ^b   Mochizuki, Masahiro ^c   Uchiumic, Toshio ^c   Ishitani, Ryuichiro ^b   Nureki, Osamu ^b   Ito, Koichi ^a  

^a Division of Molecular Biology

^b UNIVERSITY OF TOKYO   (Japan)

^c NIIGATA UNIVERSITY   (Japan)

Author keywords

Genetic code; Protein quality control; tRNA mimicy

Indexed keywords

BINDING PROTEIN; ELONGATION FACTOR; ELONGATION FACTOR 1ALPHA; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; PELOTA PROTEIN; PROTEIN HBS1; RELEASE FACTOR 1; TRANSFER RNA; UNCLASSIFIED DRUG;

AEROPYRUM PERNIX; ANIMAL CELL; ANIMAL EXPERIMENT; ARCHAEBACTERIUM; BINDING AFFINITY; CATALYSIS; COMPLEX FORMATION; CONFERENCE PAPER; CRYSTAL STRUCTURE; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; PROTEIN SYNTHESIS; QUALITY CONTROL; REGULATORY MECHANISM; STOP CODON; TRANSLATION INITIATION;

AEROPYRUM PERNIX; ARCHAEA; EUKARYOTA;

EID: 78650595932     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1009599107     Document Type: Article

References (32)

1. Nakamura Y, Ito K (2003) Making sense of mimic in translation termination. Trends Biochem Sci 28:99-105.
2. Ito K, et al. (2000) A tripeptide 'anticodon' deciphers stop codons in messenger RNA. Nature 403:680-684.
3. Frolova LY, et al. (1999) Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis. RNA 5:1014-20.
4. Laurberg M, et al. (2008) Structural basis for translation termination on the 70S ribosome. Nature 454:852-827.
5. Weixlbaumer A, et al. (2008) Insights into translational termination from the structure of RF2 bound to the ribosome. Science 322:953-956.
6. Dontsova M, et al. (2000) Translation termination factor aRF1 from the archaeon Methanococcus jannaschii is active with eukaryotic ribosomes. FEBS Lett 472:213-216.
7. Frolova L, et al. (1994) A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor. Nature 372:701-703.
8. Atkinson GC, et al. (2008) Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components. BMC Evol Biol 8:290.
9. Frolova LY, et al. (2000) Translation termination in eukaryotes: Polypeptide release factor eRF1 is composed of functionally and structurally distinct domains. RNA 6:381-390.
10. Cheng Z, et al. (2009) Structural insights into eRF3 and stop codon recognition by eRF1. Genes Dev 23:1106-1118.
11. Salas-Marco J, Bedwell DM (2004) GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination. Mol Cell Biol 24:7769-7778.
12. Lee HH, et al. (2007) Structural and functional insights into Dom34, a key component of no-go mRNA decay. Mol Cell 27:938-950.
13. Graille M, et al. (2008) Structure of yeast Dom34: A protein related to translation termination factor Erf1 and involved in No-Go decay. J Biol Chem 283:7145-7154.
14. Doma MK, Parker R (2007) RNA quality control in eukaryotes. Cell 131:660-668.
15. Kobayashi K, et al. Structural basis for ribosomal mRNA surveillance by archaeal Pelota and GTP-bound EF1α complex. Proc Natl Acad Sci USA, 107 pp:17575-17579.
16. Kawarabayashi Y, et al. (1999) Complete genome sequence of an aerobic hyperthermophilic Crenarchaeon, Aeropyrum pernix Kl. DNA Res 6:83-101.
17. Song H, et al. (2000) The crystal structure of human eukaryotic release factor eRF1- mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell 100:311-321.
18. Kong C, et al. (2004) Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. Mol Cell 14:233-245.
19. Nissen P, et al. (1995) Crystal-structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science 270:1464-1472.
20. Kawarabayashi Y, et al. (1998) Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3. DNA Res 5:55-76.
21. Nelson RJ, et al. (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71:97-105.
22. Tsuboi M, et al. (2009) EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis. Mol Cell 35:502-510.
23. Long M, et al. (2003) The origin of new genes: Glimpses from the young and old. Nature Rev Genet 4:865-875.
24. Schneider TR, Sheldrick GM (2002) Substructure solution with SHELXD. Acta Crystallogr D 58:1772-1779.
25. de La Fortelle E, Bricogne G (1997) Maximum likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol 276:472-494.
26. Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D 60:2126-2132.
27. Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D 58:1948-1954.
28. Maone E, et al. (2007) Functional analysis of the translation factor aIF2/5B in the thermophilic archaeon Sulfolobus solfataricus. Mol Microbiol 65:700-713.
29. Tate WP, Caskey CT (1990) Termination of protein synthesis. Ribosomes and Protein Synthesis: A Practical Approach, ed G Spedding (IRL Press at Oxford Univ Press, Oxford, England), pp 81-100.
30. Frolova L, et al. (1996) Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome-dependent guanosine triphosphatase. RNA 2:334-341.
31. Ito K, et al. (1998) 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.
32. DeLano WL (2002) The PyMOL Molecular Graphics System.