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Titolo:
Ribonuclease P: the diversity of a ubiquitous RNA processing enzyme
Autore:
Schon, A;
Indirizzi:
Univ Wurzburg, Biozentrum, Inst Biochem, D-97074 Wurzburg, Germany Univ Wurzburg Wurzburg Germany D-97074 iochem, D-97074 Wurzburg, Germany
Titolo Testata:
FEMS MICROBIOLOGY REVIEWS
fascicolo: 3, volume: 23, anno: 1999,
pagine: 391 - 406
SICI:
0168-6445(199906)23:3<391:RPTDOA>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRE-TRANSFER-RNA; PRECURSOR TRANSFER-RNA; ESCHERICHIA-COLI; PROTEIN SUBUNIT; SACCHAROMYCES-CEREVISIAE; PARTIAL-PURIFICATION; BACILLUS-SUBTILIS; SCHIZOSACCHAROMYCES-POMBE; ASPERGILLUS-NIDULANS; CATALYTIC CORE;
Keywords:
ribonuclease P; ribozyme; pre-tRNA processing; evolution; eukaryote; organelle;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
128
Recensione:
Indirizzi per estratti:
Indirizzo: Schon, A Univanyrzburg, Biozentrum, Inst Biochem, Am Hubland, D-97074 Wurzburg, Germ Univ Wurzburg Am Hubland Wurzburg Germany D-97074 Wurzburg, Germ
Citazione:
A. Schon, "Ribonuclease P: the diversity of a ubiquitous RNA processing enzyme", FEMS MIC R, 23(3), 1999, pp. 391-406

Abstract

Ribonuclease P is the endonuclease required for generating the mature tRNA5'-end. The ribonucleoprotein character of this enzyme has now been provenin most organisms and organelles. Exceptions, however, are still the chloroplasts, plant nuclei and animal mitochondria where no associated RNAs havebeen detected to date. In contrast to the known RNA subunits, which are fairly well-conserved in size and structure among diverse phylogenetic groups, the protein contribution to the holoenzyme is highly variable in size andnumber of the individual components. The structure of the bacterial protein component has recently been solved. In contrast, the spatial arrangement of the multiple subunits in eukaryotic enzymes is still enigmatic. Substrate requirements of the enzymes or their catalytic RNA subunits are equally diverse, ranging from simple single domain mimics to an almost intact three-dimensional structure of the pre-tRNA substrate. As an example for an intermediate in the enzyme evolution, ribonuclease P from the Cyanophora paradoxa cyanelle will be discussed in more detail. This enzyme is unique, as it combines cyanobacterial and eukaryotic features in its function, subunit composition and holoenzyme topology. (C) 1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 06:34:28