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Titolo:
RNASE P RNA FROM PROCHLOROCOCCUS-MARINUS - CONTRIBUTION OF SUBSTRATE DOMAINS TO RECOGNITION BY A CYANOBACTERIAL RIBOZYME
Autore:
HESS WR; FINGERHUT C; SCHON A;
Indirizzi:
UNIV WURZBURG,INST BIOCHEM,HUBLAND D-97074 WURZBURG GERMANY UNIV WURZBURG,INST BIOCHEM D-97074 WURZBURG GERMANY HUMBOLDT UNIV,INST BIOL D-10115 BERLIN GERMANY
Titolo Testata:
FEBS letters
fascicolo: 2, volume: 431, anno: 1998,
pagine: 138 - 142
SICI:
0014-5793(1998)431:2<138:RPRFP->2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
RIBONUCLEASE-P; M1 RNA; SEQUENCE; GENE; PRECURSORS; PROTEIN; SUBUNIT;
Keywords:
RNASE P; RIBOZYME; PRE-TRANSFER-RNA PROCESSING; TRNA(GLU); CYANOBACTERIUM; PROCHLOROCOCCUS MARINUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
W.R. Hess et al., "RNASE P RNA FROM PROCHLOROCOCCUS-MARINUS - CONTRIBUTION OF SUBSTRATE DOMAINS TO RECOGNITION BY A CYANOBACTERIAL RIBOZYME", FEBS letters, 431(2), 1998, pp. 138-142

Abstract

The molecular organisation of the Prochlorococcus marinus rnpB gene and the catalytic activity of the encoded RNA were characterised. Kinetic parameters for several pre-tRNA substrates were comparable to thosefrom other eubacterial RNase P RNAs, although unusually high cation concentrations were required. The CCA-end of pre-tRNAs is essential forefficient turnover despite the lack of the canonical binding motif inP. marinus RNase P RNA. A trnR gene is located only 38 nt upstream the rnpB 5' end on the complementary strand. This arrangement resembles those in the plastids of Cyanophora and Porphyra but not in any other bacterium. (C) 1998 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 20:11:33