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RNase P from Bacteria: Substrate recognition and the function of the protein subunit
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Microbiology. (Kirsebom)
Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla-CSIC.
1995 (English)In: Molecular Biology Reports, ISSN 0301-4851, E-ISSN 1573-4978, Vol. 22, no 2-3, 99-109 p.Article, review/survey (Refereed) Published
Abstract [en]

RNase P recognizes many different precursor tRNAs as well as other substrates and cleaves all of them accurately at the expected position. RNase P recognizes the tRNA structure of the precursor tRNA by a set of interactions between the catalytic RNA subunit and the T- and acceptor-stems mainly, although residues in the 5'-leader sequence as well as the 3'-terminal CCA are important. These conclusions have been reached by several studies on mutant precursor tRNAs as well as cross-linking studies between RNase P RNA and precursor tRNAs. The protein subunit of RNase P seems also to affect the way that the substrate is recognized as well as the range of substrates that can be used by RNase P, although the protein does not seem to interact directly with the substrates. The interaction between the protein and RNA subunits of RNase P has been extensively studied in vitro. The protein subunit sequence is not highly conserved among bacteria, however different proteins are functionally equivalent as heterologous reconstitution of the RNase P holoenzyme can be achieved in many cases.

Place, publisher, year, edition, pages
1995. Vol. 22, no 2-3, 99-109 p.
Keyword [en]
catalytic RNA, RNase P, tRNA, precursors of tRNAs, protein-RNA interaction
National Category
Natural Sciences
URN: urn:nbn:se:uu:diva-147845DOI: 10.1007/BF00988713ISI: A1996VM24800007PubMedID: 8901495OAI: oai:DiVA.org:uu-147845DiVA: diva2:400938
Available from: 2011-02-28 Created: 2011-02-28 Last updated: 2011-04-18Bibliographically approved

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