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RNase P RNA structure and cleavage reflect the primary structure of tRNA genes
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Microbiology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Microbiology. (Kirsebom)
1998 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 283, no 4, 771-783 p.Article in journal (Refereed) Published
Abstract [en]

The function of RNase P RNA depends on its folding in space. A majority of RNase P RNAs from various bacteria show a similar secondary structure to that of Escherichia coli (M1 RNA). However, there are exceptions as exemplified by the RNase P RNA derived from the low GC-content Gram-positive bacteria Bacillus subtilis and Mycoplasma hyopneumoniae (Hyo P RNA). Previous studies using M1 RNA and Hyo P RNA suggest differences both with respect to the kinetics of cleavage as well as to cleavage site recognition. Here we have studied cleavage by these two structurally different RNase P RNAs as a function of changes in the 5' leader anal the 3'-terminal CCA motif in the substrate. Our data suggest that the nucleotide at the -2 position in the 5' leader plays a role both for cleavage site recognition and for the rate of cleavage. However, depending on the identity of the -2 residue differences in the cleavage pattern comparing these two types of RNase P RNAs were observed. The results also suggest that the identity of the -1/+73 base-pair in the substrate influences the cleavage site recognition process. These findings will be related to differences in structure comparing these types of RNase P RNAs and the "RCCA-RNase P RNA" interaction. In addition, our findings will be discussed with respect to the primary structure of the tRNA genes in different bacteria.

Place, publisher, year, edition, pages
1998. Vol. 283, no 4, 771-783 p.
Keyword [en]
RNase P, ribozyme, tRNA precursors, tRNA processing
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:uu:diva-147828DOI: 10.1006/jmbi.1998.2135ISI: 000076854700006PubMedID: 9790839OAI: oai:DiVA.org:uu-147828DiVA: diva2:400911
Available from: 2011-02-28 Created: 2011-02-28 Last updated: 2011-03-01Bibliographically approved

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