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Titolo:
COOPERATIVE INTERACTIONS OF RNA AND THIOSTREPTON ANTIBIOTIC WITH 2 DOMAINS OF RIBOSOMAL-PROTEIN L11
Autore:
XING YY; DRAPER DE;
Indirizzi:
JOHNS HOPKINS UNIV,DEPT CHEM,CHARLES & 34TH ST BALTIMORE MD 21218 JOHNS HOPKINS UNIV,DEPT CHEM BALTIMORE MD 21218
Titolo Testata:
Biochemistry
fascicolo: 5, volume: 35, anno: 1996,
pagine: 1581 - 1588
SICI:
0006-2960(1996)35:5<1581:CIORAT>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
CONSERVED GTPASE CENTER; ELONGATION-FACTOR-G; N-TERMINAL DOMAIN; RELEASE FACTOR-I; ESCHERICHIA-COLI; ARCHAEBACTERIAL RIBOSOMES; SACCHAROMYCES-CEREVISIAE; BACILLUS-MEGATERIUM; BINDING-SITE; 23S RNA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
Y.Y. Xing e D.E. Draper, "COOPERATIVE INTERACTIONS OF RNA AND THIOSTREPTON ANTIBIOTIC WITH 2 DOMAINS OF RIBOSOMAL-PROTEIN L11", Biochemistry, 35(5), 1996, pp. 1581-1588

Abstract

Ribosomal protein L11 interacts with a SX-nucleotide domain of large subunit ribosomal RNA; both the protein and its RNA target have been highly conserved. The antibiotic thiostrepton recognizes the same RNA domain, and binds to the ribosome cooperatively with L11. Experiments presented here show that RNA recognition and thiostrepton cooperativitycan be attributed to C- and N-terminal domains of L11, respectively. Under trypsin digestion conditions that degrade Bacillus stearothermophilus L11 to small fragments, the target RNA protects the C-terminal 77 residues from digestion, and thiostrepton and RNA in combination protect the entire protein. A 76-residue C-terminal fragment of L11 was overexpressed and shown to fold into a stable structure binding ribosomal RNA with essentially the same properties as full-length L11. An L11. thiostrepton . RNA complex was 100-200-fold more stable than expected on the basis of L11-RNA and thiostrepton-RNA binding affinities; similar measurements with the C-terminal fragment detected no cooperativity with thiostrepton. L11 function is thus more complex than simple interaction with ribosomal RNA; we suggest that thiostrepton mimics some ribosomal component or factor that normally interacts with the L11 N-terminal domain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 15:14:27