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Titolo:
The contribution of a zinc finger motif to the function of yeast ribosomalprotein YL37a
Autore:
Rivlin, AA; Chan, YL; Wool, IG;
Indirizzi:
Univ Chicago, Dept Biochem & Mol Biol, Chicago, IL 60637 USA Univ ChicagoChicago IL USA 60637 ochem & Mol Biol, Chicago, IL 60637 USA
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 4, volume: 294, anno: 1999,
pagine: 909 - 919
SICI:
0022-2836(199912)294:4<909:TCOAZF>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTION FACTOR-IIIA; HIGH-LEVEL EXPRESSION; ESCHERICHIA-COLI; SACCHAROMYCES-CEREVISIAE; DNA-BINDING; EUKARYOTIC GENES; RNA-POLYMERASE; RECOGNITION; L25; COMPLEX;
Keywords:
ribosomal proteins; yeast YL37a; zinc finger motif;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Wool, IG Univ Chicago, Dept Biochem & Mol Biol, Chicago, IL 60637 USA UnivChicago Chicago IL USA 60637 ol Biol, Chicago, IL 60637 USA
Citazione:
A.A. Rivlin et al., "The contribution of a zinc finger motif to the function of yeast ribosomalprotein YL37a", J MOL BIOL, 294(4), 1999, pp. 909-919

Abstract

Eukaryotic ribosomes have a large number of proteins but the exact nature of their contribution to the structure and to the function of the particle is not known. Of the 78 proteins in yeast ribosomes, six have zinc finger motifs of the C-2-C-2 variety. Both genes encoding the essential yeast ribosomal protein YL37a, which has such a zinc finger motif, were disrupteXXPd. The double deletion, which is lethal, can be rescued with a plasmid-encodedcopy of a YL37a gene. Mutations were constructed in a plasmid-encoded copyof YL37a; the mutations caused the cysteine residues in the motif (at positions 39, 42, 57 and 60) to be replaced, one at a time, with serine. The cysteine residue at position 39, the first of the four in the motif, is essential for the function of YL37a, since a C39S mutation did not complement the null phenotype. However, plasmids encoding variants with C42S, C57S, or C60S mutations in the zinc finger motif were able to rescue the null mutant. YL37a binds zinc, but none of the mutant proteins, C39S, C42S, C57S, or C60S, was able to bind the metal. Thus, all four cysteine residues are essential for the binding of zinc; only one, C39, is essential for the function of the ribosomal protein. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:53:08