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Titolo:
Mechanism of tRNA translocation on the ribosome
Autore:
Rodnina, MV; Semenkov, YP; Savelsbergh, A; Katunin, VI; Peske, F; Wilden, B; Wintermeyer, W;
Indirizzi:
Univ Witten Herdecke, Inst Phys Biochem, D-58448 Witten, Germany Univ Witten Herdecke Witten Germany D-58448 hem, D-58448 Witten, Germany Russian Acad Sci, St Petersburg Nucl Phys Inst, Gatchina 188350, Russia Russian Acad Sci Gatchina Russia 188350 ys Inst, Gatchina 188350, Russia Univ Witten Herdecke, Inst Mol Biol, D-58448 Witten, Germany Univ Witten Herdecke Witten Germany D-58448 iol, D-58448 Witten, Germany
Titolo Testata:
MOLECULAR BIOLOGY
fascicolo: 4, volume: 35, anno: 2001,
pagine: 559 - 568
SICI:
0026-8933(200107/08)35:4<559:MOTTOT>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELONGATION-FACTOR-G; FLUORESCENCE ENERGY-TRANSFER; ESCHERICHIA-COLI RIBOSOMES; ALLOSTERIC 3-SITE MODEL; PEPTIDYL-TRANSFER-RNA; 70S RIBOSOME; EXIT SITE; PROMOTES TRANSLOCATION; CRYSTAL-STRUCTURE; GTP HYDROLYSIS;
Keywords:
protein synthesis; GTPase; motor protein; tRNA translocation; hybrid states; kinetics; catalysis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Rodnina, MV Univ Witten Herdecke, Inst Phys Biochem, D-58448 Witten, Germany Univ Witten Herdecke Witten Germany D-58448 Witten, Germany
Citazione:
M.V. Rodnina et al., "Mechanism of tRNA translocation on the ribosome", MOL BIOL, 35(4), 2001, pp. 559-568

Abstract

During the translocation step of the elongation cycle of peptide synthesistwo tRNAs together with the mRNA move synchronously and rapidly on the ribosome. Translocation is catalyzed by the elongation factor G (EF-G) and requires GTP hydrolysis. The fundamental biochemical features of the process were worked out in the 1970-80s, to a large part by A.S. Spirin and his colleagues. Recent results from pre-steady-state kinetic analysis and cryoelectron microscopy suggest that translocation is a multistep dynamic process that entails large-scale structural rearrangements of both ribosome and EF-G. Kinetic and thermodynamic data, together with the structural information on the conformational changes in the ribosome and EF-G, provide a detailed mechanistic model of translocation and suggest a mechanism of translocation catalysis by EF-G.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 23:28:47