Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A ratchet-like inter-subunit reorganization of the ribosome during translocation
Autore:
Frank, J; Agrawal, RK;
Indirizzi:
SUNY Albany, Howard Hughes Med Inst, Albany, NY 12201 USA SUNY Albany Albany NY USA 12201 ard Hughes Med Inst, Albany, NY 12201 USA SUNY Albany, Wadsworth Ctr, Hlth Res Inc, Albany, NY 12201 USA SUNY Albany Albany NY USA 12201 h Ctr, Hlth Res Inc, Albany, NY 12201 USA SUNY Albany, Dept Biomed Sci, Albany, NY 12201 USA SUNY Albany Albany NY USA 12201 ny, Dept Biomed Sci, Albany, NY 12201 USA
Titolo Testata:
NATURE
fascicolo: 6793, volume: 406, anno: 2000,
pagine: 318 - 322
SICI:
0028-0836(20000720)406:6793<318:ARIROT>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI RIBOSOME; ELONGATION-FACTOR-G; 70S RIBOSOME; CRYOELECTRON MICROSCOPY; ANGSTROM RESOLUTION; TRANSFER-RNAS; EF-TU; VISUALIZATION; MOVEMENT; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Frank, J SUNY Albany, Howard Hughes Med Inst, Empire State Plaza,POB 509, Albany, NY 12201 USA SUNY Albany Empire State Plaza,POB 509 Albany NY USA 12201 01 USA
Citazione:
J. Frank e R.K. Agrawal, "A ratchet-like inter-subunit reorganization of the ribosome during translocation", NATURE, 406(6793), 2000, pp. 318-322

Abstract

The ribosome is a macromolecular assembly that is responsible for protein biosynthesis following genetic instructions in all organisms. It is composed of two unequal subunits: the smaller subunit binds messenger RNA and the anticodon end of transfer RNAs, and helps to decode the mRNA; and the larger subunit interacts with the amino-acid-carrying end of tRNAs and catalysesthe formation of the peptide bonds. After peptide-bond formation, elongation factor G (EF-G) binds to the ribosome, triggering the translocation of peptidyl-tRNA from its aminoacyl site to the peptidyl site, and movement of mRNA by one codon(1). Here we analyse three-dimensional cryo-electron microscopy maps of the Escherichia coli 70S ribosome in various functional states, and show that both EF-G binding and subsequent GTP hydrolysis lead to ratchet-like rotations of the small 30S subunit relative to the large 50S subunit. Furthermore, our finding indicates a two-step mechanism of translocation: first, relative rotation of the subunits and opening of the mRNA channel following binding of GTP to EF-G; and second, advance of the mRNA/(tRNA)(2) complex in the direction of the rotation of the 30S subunit, following GTP hydrolysis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/04/20 alle ore 10:50:25