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PMID: 358197 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Ribonuclease P: an enzyme with an essential RNA component.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 8 ·1978-08-00 ·Pages 3717-21

Stark BC, Kole R, Bowman EJ, Altman S

Abstract

The activity of ribonuclease P on precursor tRNA substrates from Escherichia coli can be abolished by pretreatment of this enzyme with micrococcal nuclease or pancreatic ribonuclease A, as well as by proteases and by thermal denaturation. Highly purified RNase P exhibits one prominent RNA and one 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.

MeSH Terms
Chemical Phenomena Chemistry Endonucleases Escherichia coli Models, Chemical Molecular Weight RNA/analysis RNA, Transfer/metabolism Ribonucleases
Chemicals
RNA RNA, Transfer Endonucleases Ribonucleases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Stark B C
Kole R
Bowman E J
Altman S
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25 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.75.8.3717
Published
1978-08-00
Pages
3717-21
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC392857
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.75.8.3717 PMC Full Text View journal details
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