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Nucleic Acids Research, Vol 24, Issue 8 1497-1503, Copyright © 1996 by Oxford University Press

ARTICLES

The catalytic core of RNase P

CJ Green, R Rivera-Leon and BS Vold
SRI International, Menlo Park, CA 94025-3493, USA.

A deletion mutant of the catalytic RNA component of Escherichia coli RNase P missing residues 87-241 retains the ability to interact with the protein component to form a functional catalyst. The deletion of this phylogenetically conserved region significantly increases the Km, indicating that the deleted structures may be important for binding to the precursor tRNA substrate but not for the cleavage reaction. Under some reaction conditions, this RNase P deletion mutant can become a relatively non-specific nuclease, indicating that this RNA's catalytic center may be more exposed. The catalytic core of the RNase P is formed by less than one third of the 377 residues of the RNase P RNA.
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