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RNase P RNA-mediated cleavage
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
2009 (English)In: IUBMB Life - A Journal of the International Union of Biochemistry and Molecular Biology, ISSN 1521-6543, E-ISSN 1521-6551, Vol. 61, no 3, 189-200 p.Article, review/survey (Refereed) Published
Abstract [en]

Metal(II)-induced hydrolysis of RNA produce products with 5'-hydroxyls and 2';3'-cyclic phosphates at the ends. Ribozymes are RNA molecules that act as catalysts. Some ribozymes that cleave RNA also generate 5-hydroxyls and 2';3-cyclic phosphates whereas others produces 5-phosphates and 5'-hydroxyls at the ends of the cleavage products. RNase P is an essential endoribonuclease involved in RNA processing. The catalytic RNA subunit or RNase P is a trans-acting ribozyme that cleaves various RNA substrates in vitro generating 5'-phosphates and Y-hydroxyls as cleavage products. The activity depends on the presence of metal(II) ions such as Mg2+. RNase P RNA has therefore to facilitate a nucleophilic attack that generates the correct product ends and prevent metal(II)-induced hydrolysis of the RNA substrate. In this review, we will discuss our current understanding of the interactions between RNase P RNA and its substrate, role of specific residues with respect to catalysis and positioning of functionally important Mg2+ at and in the vicinity of the cleavage site that ensures that products with correct ends are generated. Moreover, we will discuss the composition of RNase P and its RNA subunit in an evolutionary perspective.

Place, publisher, year, edition, pages
2009. Vol. 61, no 3, 189-200 p.
Keyword [en]
RNase P, ribozyme, divalent metal ions, tRNA precursors, tRNA processing
National Category
Biochemistry and Molecular Biology
Research subject
Microbiology
Identifiers
URN: urn:nbn:se:uu:diva-106200DOI: 10.1002/iub.160ISI: 000264089500001PubMedID: 19243011OAI: oai:DiVA.org:uu-106200DiVA: diva2:224227
Available from: 2009-06-17 Created: 2009-06-17 Last updated: 2011-03-07Bibliographically approved

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