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Titolo:
The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22
Autore:
Gabashvili, IS; Gregory, ST; Valle, M; Grassucci, R; Worbs, M; Wahl, MC; Dahlberg, AE; Frank, J;
Indirizzi:
SUNY Albany, Wadsworth Ctr Labs & Res, Albany, NY 12201 USA SUNY Albany Albany NY USA 12201 orth Ctr Labs & Res, Albany, NY 12201 USA 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, Dept Biomed Sci, Albany, NY 12201 USA SUNY Albany Albany NY USA 12201 ny, Dept Biomed Sci, Albany, NY 12201 USA Brown Univ, Div Biol & Med, Dept Mol & Cell Biol & Biochem, Providence, RI02912 USA Brown Univ Providence RI USA 02912 iol & Biochem, Providence, RI02912 USA Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany Max Planck Inst Biochem Martinsried Germany D-82152 Martinsried, Germany
Titolo Testata:
MOLECULAR CELL
fascicolo: 1, volume: 8, anno: 2001,
pagine: 181 - 188
SICI:
1097-2765(200107)8:1<181:TPTSIT>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLI 70S RIBOSOME; RNA-BINDING-SITES; ESCHERICHIA-COLI; CRYOELECTRON MICROSCOPY; ANGSTROM RESOLUTION; CONFORMATIONAL SWITCH; ELECTRON-MICROSCOPY; CRYSTAL-STRUCTURE; PROTEIN; SUBUNIT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Frank, J SUNY Albany, Wadsworth Ctr Labs & Res, POB 509, Albany, NY 12201 USA SUNY Albany POB 509 Albany NY USA 12201 509, Albany, NY 12201 USA
Citazione:
I.S. Gabashvili et al., "The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22", MOL CELL, 8(1), 2001, pp. 181-188

Abstract

Variations in the inner ribosomal landscape determining the topology of nascent protein transport have been studied by three-dimensional cryo-electron microscopy of erythromycin-resistant Escherichia coli 70S ribosomes. Significant differences in the mouth of the 50S subunit tunnel system visualized in the present study support a simple steric-hindrance explanation for the action of the drug. Examination of ribosomes in different functional states suggests that opening and closing of the main tunnel are dynamic features of the large subunit, possibly accompanied by changes in the L7/L12 stalkregion. The existence and dynamic behavior of side tunnels suggest that ribosomal proteins L4 and L22 might be involved in the regulation of a multiple exit system facilitating cotranslational processing (or folding or directing) of nascent proteins.

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Documento generato il 22/01/20 alle ore 12:43:22