Abstract
The elongation phase of translation leads to the decoding of the mRNA and the synthesis of the corresponding polypeptide chain. In most eukaryotes, two distinct protein elongation factors (eEF-1 and eEF-2) are required for elongation. Each is active as a complex with GTP. eEF-1 is a multimer and mediates the binding of the cognate aminoacyl-tRNA to the ribosome, while eEF-2, a monomer, catalyses the movement of the ribosome relative to the mRNA. Recent work showing that bacterial ribosomes possess three sites for tRNA binding and that during elongation tRNAs may occupy ‘hybrid’ sites is incorporated into a model of eukaryotic elongation. In fungi, elongation also requires a third factor, eEF-3. A number of mechanisms exist to promote the accuracy or ‘fidelity’ of elongation: eEF-3 may play a role here. cDNAs for this and the other elongation factors have been cloned and sequenced, and the structural and functional properties of the elongation factors are discussed. eEF-1 and eEF-2 can be regulated by phosphorylation, and this may serve to control rates of elongationin vivo.
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Abbreviations
- eEF:
-
eukaryotic elongation factor-
- PKC:
-
protein kinase C
References
Giegé R, Puglisi JD & Florentz C (1993) Prog. Nucleic Acids Res. and Mol. Biol. 45: 129–206
Schulman LH (1991) Prog. Nucleic Acids Res. and Mol. Biol. 41: 23–87
Böck A, Forchhammer K, Heider J, Leinfelder W, Sawers G, Veprek B & Zinoni F (1991) Mol. Microbiol. 5: 515–520
Riis B, Rattan SIS, Clark BFC & Merrick WC (1990) Trends Biochem. Sci. 15: 420–424
Belfield GP & Tuite MF (1993) Mol. Microbiol. 9: 411–418
Slobin LJ & Möller W (1975) Nature 258: 452–454
Weissbach H, Redfield B & Moon H-M (1973) Arch. Biochem. Biophys. 156: 267–275
Crechet J-B & Parmeggiani A (1986) Eur. J. Biochem. 161: 655–660
Janssen GMC & Möller W (1988) J. Biol. Chem. 263: 1773–1778
Van Damme H, Amons R, Karssies R, Timmers CJ, Janssen GMC & Möller W (1990) Biochim. Biophys. Acta 1050: 241–247
Cormier P, Osborne HB, Morales J, Bassez T, Minella O, Poulhe R, Bellé R & Mulner-Lorillon O (1993) Nucleic Acids Res. 21: 743
Van Damme H, Amons R, Janssen G & Möller W (1991) Eur. J. Biochem. 197: 505–511
Sanders J, Raggiaschi R, Morales J & Möller W (1993) Biochim. Biophys. Acta 1174: 87–90
Hiraga K, Suzuki K, Tsuchiya E & Miyakawa T (1993) FEBS Lett. 316: 165–169
Venema RC, Peters HI & Traugh JA (1991) J. Biol. Chem. 266: 11993–11998
Venema RC, Peters HI & Traugh JA (1991) J. Biol. Chem. 266: 12574–12580
Janssen GMC, Maessen GDF, Amons R & Möller W (1988) J. Biol. Chem. 263: 11063–11066
Cavallius J, Zoll W, Chakraburtty K & Merrick WC (1993) Biochim. Biophys. Acta 1163: 75–80
Weijland A, Harmark K, Cool RH, Anborgh PH & Parmeggiani A (1992) Mol. Microbiol. 6: 683–688
Weijland A & Parmeggiani A (1993) Science 259: 1311–1314
Song JM, Picologlou S, Grant CM, Firoozan M, Tuite MF & Liebman S (1989) Mol. Cell. Biol. 9: 4571–4575
Shepherd JCW, Walldorf U, Hug P & Gehring WJ (1989) Proc. Natl. Acad. Sci. USA 86: 7520–7521
Cavallius J, Rattan SIS & Clark BFC (1986) Exp. Gerontol. 21: 149–157
Tatsuka M, Mitsui H, Wada M, Nagata A, Nojima H & Okayama H (1992) Nature 359: 333–336
Rao MN & Slobin LI (1986) Mol. Cell. Biol. 7: 687–697
Thomas G & Thomas G (1986) J. Cell Biol. 103: 2137–2144
Slobin LI & Rao MN (1993) Eur. J. Biochem. 213: 919–926
Taniguchi S, Miyamoto S, Sadano H & Kobayashi H (1991) Nucleic Acids Res. 19: 6949
Deleted in proof.
Riis B, Rattan SIS, Clark BFC & Merrick WC (1990) Trends Biochem. Sci. 15: 420–424
Nygård O & Nilsson L (1989) Eur. J. Biochem. 179: 603–608
Corquet F, Lavergne J-P, Paleologue A, Reboud J-P & Reboud A-M (1987) Eur. J. Biochem. 163: 15–20
Nygård O & Nilsson L (1990a) Eur. J. Biochem. 191: 1–17
Tanaka M, Iwasaki K & Kaziro Y (1977) J. Biochem. 82: 1035–1043
Phan LD, Parentesis JP & Bodley JW (1993) J. Biol. Chem. 268: 8665–8668
Nygård O & Nilsson L (1990) J. Biol. Chem. 265: 6030–6034
Marzouki A, Sontag B, Lavergne JP, Vidonne C, Reboud JP & Reboud AM (1991) Biochimie 73: 1151–1156
Price NT, Redpath NT, Severinov KV, Campbell DG, Russell R & Proud CG (1991) FEBS Lett. 282: 253–258
Redpath NT, Price NT, Severinov KV & Proud CG (1993) Eur. J. Biochem. 213: 689–699
Nairn AC & Palfrey HC (1987) J. Biol. Chem. 262: 17299–17303
Ryazanov AG, Shestakova EA & Natapov PG (1988) Nature (London) 334: 170–173
Nairn AC, Bhagat B & Palfrey HC (1985) Proc. Natl. Acad. Sci. USA 82: 7939–7943
Redpath NT & Proud C G (1993a) Eur. J. Biochem. 212: 511–520
Redpath NT & Proud CG (1993b) Biochem. J. 293: 31–34
Davydova EK, Malinin NL & Ovchinnikov LP (1993) Eur. J. Biochem. 215: 291–296
Miyazaki M, Uritani M, Kitaoka Y, Ogawa K & Kagiyama H (1990) in Post-transcriptional control of gene expression. McCarthy JEG & Tuite MF (eds.) Berlin: Springer-Verlag, pp. 557–566
Piepersberg W, Noseda V & Böck A (1979) Mol. Gen. Genet. 171: 23–34
Colthurst DR, Belfield GP & Tuite MF (1991) Biochem. Soc. Trans. 19: 279S
Skogerson L & Wakatama E (1976) Proc. Natl. Acad. Sci. USA 73: 73–76
Qin S, Moldave K & McLaughlin CS (1986) J. Biol. Chem. 262: 7802–2807
Uritani M & Miyazaki M (1988) J. Biochem. 104: 118–126
Traut RR & Monro RE (1964) J. Mol. Biol. 11: 35–53
Rheinberger HJ (1991) Biochimie 73: 1067–1088
Moazed D & Noller HF (1989) Nature (London) 342: 142–148
Hopfield JJ (1974) Proc. Natl. Acad. Sci. USA 71: 4135–4139
Ninio J (1975) Biochimie 57: 587–595
Robin D & Hardesty B (1983) Biochemistry 22: 5675–5679
Rheinberger HJ, Sternbach H & Nierhaus KH (1981) Proc. Natl. Acad. Sci. USA 78: 5310–5314
Modollel J & Davis BD (1968) Proc. Natl. Acad. Sci. USA 61: 1279–1286
Rheinberger HJ & Nierhaus KH (1983) Proc. Natl. Acad. Sci. USA 80, 4213–4217
Wettstein FO & Noll H (1965) J. Mol. Biol. 11: 35–53
Rodnina MV, El'skaya AV, Semenkov YP & Kirillov SV (1988) FEBS Lett. 231: 71–74
Merrick WC (1992) Microbiol. Rev. 56: 291–315
Odom OW & Hardesty B (1987) Biochimie 69: 925–938
Matzke AJM, Barta A & Kuechler E (1980) Proc. Natl. Acad. Sci. USA 77: 5110–5114
Beletsina NV & Spirin AS (1979) Eur. J. Biochem. 94: 315–320
Robertson JM & Wintermeyer W (1989) American Society for Microbiology Conference on Ribosomes. Abstract II-12, Montana
Lill R, Robertson JM & Wintermeyer W (1984) Biochemistry 23: 6710–6717
Holschuh K & Gassen HG (1982) J. Biol. Chem. 257: 1987–1992
Nierhaus KH (1984) Mol. Cell. Biochem. 61: 63–81
Pinna LA (1990) Biochim. Biophys. Acta 1054: 267–284
Proud CG (1992) Curr. Topics Cell. Regul. 32: 243–369
Ayuso-Parrilla MS, Martin-Requero A, Perez-Diaz J & Parrilla R (1976) J. Biol. Chem. 251: 7785–7790
Nielsen PJ & McConkey EH (1980) J. Cell. Physiol. 104: 269–281
Hassell JA & Engelhardt DL (1976) Biochemistry 15: 1375–1381
Fischer I, Arfin SM & Moldave K (1980) Biochemistry 19: 1417–1425
Ramabhandran TV & Thach RE (1981) J. Virol. 39: 573–583
Brandis JW & Raff RA (1979) Nature 278: 467–469
Hille MB & Albers AA (1979) Nature 278: 469–471
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Proud, C.G. Peptide-chain elongation in eukaryotes. Mol Biol Rep 19, 161–170 (1994). https://doi.org/10.1007/BF00986958
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DOI: https://doi.org/10.1007/BF00986958