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Titolo:
The Tat protein export pathway
Autore:
Berks, BC; Sargent, F; Palmer, T;
Indirizzi:
Univ E Anglia, Sch Biol Sci, Ctr Met Prot Spect & Biol, Norwich NR4 7TJ, Norfolk, England Univ E Anglia Norwich Norfolk England NR4 7TJ h NR4 7TJ, Norfolk, England John Innes Ctr Plant Sci Res, Dept Mol Microbiol, Norwich NR4 7UH, Norfolk, England John Innes Ctr Plant Sci Res Norwich Norfolk England NR4 7UH olk, England
Titolo Testata:
MOLECULAR MICROBIOLOGY
fascicolo: 2, volume: 35, anno: 2000,
pagine: 260 - 274
SICI:
0950-382X(200001)35:2<260:TTPEP>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
DELTA-PH PATHWAY; GLUCOSE-FRUCTOSE OXIDOREDUCTASE; ESCHERICHIA-COLI HYDROGENASE-2; CRYSTAL-STRUCTURE; SIGNAL PEPTIDE; THYLAKOID MEMBRANES; DEHALOSPIRILLUM MULTIVORANS; STREPTOMYCES TYROSINASE; SHEWANELLA-PUTREFACIENS; FORMATE DEHYDROGENASE;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
93
Recensione:
Indirizzi per estratti:
Indirizzo: Berks, BC Univ E Anglia, Sch Biol Sci, Ctr Met Prot Spect & Biol, Norwich NR4 7TJ, Norfolk, England Univ E Anglia Norwich Norfolk England NR4 7TJ Norfolk, England
Citazione:
B.C. Berks et al., "The Tat protein export pathway", MOL MICROB, 35(2), 2000, pp. 260-274

Abstract

The Tat (twin-arginine translocation) system is a bacterial protein exportpathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operationof this major new bacterial protein export pathway.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/08/20 alle ore 13:42:58