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Science 8 January 1988:
Vol. 239. no. 4836, pp. 178 - 181
DOI: 10.1126/science.3122322
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Articles

Science, Vol 239, Issue 4836, 178-181
Copyright © 1988 by American Association for the Advancement of Science

articles

Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme

C Reich, GJ Olsen, B Pace, and NR Pace

Department of Biology, Indiana University, Bloomington 47405.

The Bacillus subtilis ribonuclease P consists of a protein and an RNA. At high ionic strength the reaction is protein-independent; the RNA alone is capable of cleaving precursor transfer RNA, but the turnover is slow. Kinetic analyses show that high salt concentrations facilitate substrate binding in the absence of the protein, probably by decreasing the repulsion between the polyanionic enzyme and substrate RNAs, and also slow product release and enzyme turnover. It is proposed that the ribonuclease P protein, which is small and basic, provides a local pool of counter-ions that facilitates substrate binding without interfering with rapid product release.


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