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Nucleic Acids Research, 2002, Vol. 30, No. 23 5065-5073
© 2002 Oxford University Press

Elucidation of structure–function relationships in the protein subunit of bacterial RNase P using a genetic complementation approach

Milan Jovanovic1,2, Ruth Sanchez3, Sidney Altman3 and Venkat Gopalan*,1,2

1 Department of Biochemistry and 2 The Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA and 3 Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520-8103, USA

*To whom correspondence should be addressed. Tel: +1 614 292 1332; Fax: +1 614 292 6773; Email: gopalan.5{at}osu.edu

RNase P is a ribonucleoprotein involved in tRNA biosynthesis in all living organisms. Bacterial RNase P is comprised of a catalytic RNA subunit and a lone protein cofactor which plays a supporting, albeit essential, role in the tRNA processing reaction in vivo. In this study, we have searched various databases to identify homologs of the protein subunit of RNase P from diverse bacteria and used an alignment of their primary sequences to determine the most highly conserved residues, and thereby extend earlier predictions of which residues might play an important role in RNA recognition. By employing a genetic complementation assay, we have also gained insights into structure– function relationships in the protein subunit of bacterial RNase P.


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