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Titolo:
SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA)
Autore:
Karzai, AW; Susskind, MM; Sauer, RT;
Indirizzi:
MIT, Dept Biol, Cambridge, MA 02139 USA MIT Cambridge MA USA 02139MIT, Dept Biol, Cambridge, MA 02139 USA Univ So Calif, Dept Biol Sci, Los Angeles, CA 90089 USA Univ So Calif LosAngeles CA USA 90089 iol Sci, Los Angeles, CA 90089 USA
Titolo Testata:
EMBO JOURNAL
fascicolo: 13, volume: 18, anno: 1999,
pagine: 3793 - 3799
SICI:
0261-4189(19990701)18:13<3793:SAURPE>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
SMALL STABLE RNA; ESCHERICHIA-COLI TMRNA; ELONGATION-FACTOR-G; 10SA RNA; BACTERIOPHAGE-LAMBDA; CRYSTAL-STRUCTURE; MESSENGER-RNA; Q-GENE; PROMOTER; SYSTEM;
Keywords:
10Sa RNA; phage development; protein degradation; ribosome association; translation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Sauer, RT MIT, Dept Biol, 77 Massachusetts Ave, Cambridge, MA 02139 USA MIT 77 Massachusetts Ave Cambridge MA USA 02139 ge, MA 02139 USA
Citazione:
A.W. Karzai et al., "SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA)", EMBO J, 18(13), 1999, pp. 3793-3799

Abstract

In bacteria, SsrA RNA recognizes ribosomes stalled on defective messages and acts as a tRNA and mRNA to mediate the addition of a short peptide tag to the C-terminus of the partially synthesized nascent polypeptide chain. The SsrA-tagged protein is then degraded by C-terminal-specific proteases. SmpB, a unique RNA-binding protein that is conserved throughout the bacterialkingdom, is shown here to be an essential component of the SsrA quality-control system. Deletion of the smpB gene in Escherichia coli results in the same phenotypes observed in ssrA-defective cells, including a variety of phage development defects and the failure to tag proteins translated from defective mRNAs. Purified SmpB binds specifically and with high affinity to SsrA RNA and is required for stable association of SsrA with ribosomes in vivo. Formation of an SmpB-SsrA complex appears to be critical in mediating SsrA activity after aminoacylation with alanine but prior to the transpeptidation reaction that couples this alanine to the nascent chain. SsrA RNA is present at wild-type levels in the smpB mutant arguing against a model of SsrA action that involves direct competition for transcription factors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 06:55:36