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Titolo:
Visualization of protein S1 within the 30S ribosomal subunit and its interaction with messenger RNA
Autore:
Sengupta, J; Agrawal, RK; Frank, J;
Indirizzi:
New York State Dept Hlth, Wadsworth Ctr, Albany, NY 12201 USA New York State Dept Hlth Albany NY USA 12201 th Ctr, 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 Hlth Res Inc, Howard Hughes Med Inst, Albany, NY 12201 USA Hlth Res Inc Albany NY USA 12201 rd Hughes Med Inst, Albany, NY 12201 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 21, volume: 98, anno: 2001,
pagine: 11991 - 11996
SICI:
0027-8424(20011009)98:21<11991:VOPSWT>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLI 70S RIBOSOME; ESCHERICHIA-COLI; ANGSTROM RESOLUTION; CRYOELECTRON MICROSCOPY; ELECTRON-MICROSCOPY; BINDING PROPERTIES; 30-S SUBUNIT; DENSITY MAPS; 16S RNA; 3' END;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Frank, J New York State Dept Hlth, Wadsworth Ctr, Empire State Plaza, Albany, NY 12201 USA New York State Dept Hlth Empire State Plaza Albany NY USA 12201 A
Citazione:
J. Sengupta et al., "Visualization of protein S1 within the 30S ribosomal subunit and its interaction with messenger RNA", P NAS US, 98(21), 2001, pp. 11991-11996

Abstract

S1 is the largest ribosomal protein, present in the small subunit of the bacterial ribosome. It has a pivotal role in stabilizing the mRNA on the ribosome. Thus far, S1 has eluded structural determination. We have identifiedthe S1 protein mass in the cryo-electron microscopic map of the Escherichia coli ribosome by comparing the map with a recent x-ray crystallographic structure of the 30S subunit, which lacks S1. According to our finding, S1 is located at the junction of head, platform, and main body of the 30S subunit, thus explaining all existing biochemical and crosslinking data. ProteinS1 as identified in our map has a complex, elongated shape with two holes in its central portion. The IN-terminal domain, forming one of the extensions, penetrates into the head of the 30S subunit. Evidence for direct interaction of S1 with 11 nucleotides of the mRNA, immediately upstream of the Shine-Dalgarno sequence, explains the protein's role in the recognition of the 5' region of mRNA.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 21:50:33