Ribonuclease P: an enzyme with an essential RNA component.
- 1 August 1978
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 75 (8), 3717-3721
- https://doi.org/10.1073/pnas.75.8.3717
Abstract
The activity of RNase P on precursor tRNA substrates from Escherichia coli can be abolished by pretreatment of this enzyme with micrococcal nuclease or pancreatic RNase A, and by proteases and by thermal denaturation. Highly purified RNase P exhibits 1 prominent RNA and 1 prominent polypeptide component when examined in polyacrylamide gels containing sodium dodecyl sulfate. The buoyant density in CsCl of RNase P, 1.71 g/ml, is characteristic of a protein-RNA complex. The activity of RNase P is inhibited by various RNA molecules. The presence of a discrete RNA component in RNAse P appears to be essential for enzymatic function. A model is described for enzyme-substrate recognition in which this RNA component plays an important role.This publication has 25 references indexed in Scilit:
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