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Titolo:
Cyanelle RNase P: RNA structure analysis and holoenzyme properties of an organellar ribonucleoprotein enzyme
Autore:
Cordier, A; Schon, A;
Indirizzi:
Univ Wurzburg, Inst Biochem, Biozentrum, D-97074 Wurzburg, Germany Univ Wurzburg Wurzburg Germany D-97074 entrum, D-97074 Wurzburg, Germany
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 1, volume: 289, anno: 1999,
pagine: 9 - 20
SICI:
0022-2836(19990528)289:1<9:CRPRSA>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR RIBONUCLEASE-P; ESCHERICHIA-COLI; PROTEIN SUBUNIT; M1 RNA; ASPERGILLUS-NIDULANS; PARTIAL-PURIFICATION; RIBOSOMAL-RNA; SUBSTRATE; SEQUENCE; RECOGNITION;
Keywords:
chloroplast; evolution; pre-tRNA processing; ribonuclease P; structure probing;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Schon, A Univ Wurzburg, Inst Biochem, Biozentrum, Hubland, D-97074 Wurzburg, Germany Univ Wurzburg Hubland Wurzburg Germany D-97074 Wurzburg, Germany
Citazione:
A. Cordier e A. Schon, "Cyanelle RNase P: RNA structure analysis and holoenzyme properties of an organellar ribonucleoprotein enzyme", J MOL BIOL, 289(1), 1999, pp. 9-20

Abstract

The cyanelle of the primitive alga Cyanophora paradoxa is the only photosynthetic organelle where the ribonucleoprotein nature of ribonuclease P has been functionally proven. To increase our knowledge about RNA structure andoverall composition of this enzyme, we have now determined relevant physical parameters and performed RNA accessibility experiments. Buoyant density and relative molecular mass of cyanelle RNase P were more similar to the eukaryotic (nuclear or mitochondrial) than to the bacterial enzyme type, despite the close phylogenetic relationship between plastids and cyanobacteria. Enzymatic and chemical probing was used to establish the secondary structure of cyanelle RNase P RNA. The results obtained with the naked transcript support the previously proposed, phylogenetically derived structure. Probing of the RNA in the holoenzyme resulted in reduced sensitivity at a large number of positions, indicating that these regions might be located in the interior of the ribonucleoprotein. Protection of the RNA in cyanelle RNase Pwas more extensive than reported for the Escherichia coli holoenzyme, but similar to the pattern observed in yeast nuclear RNase P. Taken together, these results indicate that the protein contribution in cyanelle RNase P is much larger than in the bacterial enzymes, and that the overall compositionof the holoenzyme resembles that found in eukaryotes. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 23:02:59