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

Claudia Reich, Gary J. Olsen, Bernadette Pace, Norman R. Pace

Research output: Contribution to journalArticlepeer-review


The Bacillus subtilis ribonucleasc P consists of a protein and an RNA. At high ionic strength the reaction is protein-independent; die 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 die polyanionic enzyme and substrate RNAs, and also slow product release and enzyme turnover. It is proposed that die ribonuclease P protein, which is small and basic, provides a local pool of counter-ions diat facilitates substrate binding without interfering with rapid product release.

Original languageEnglish (US)
Pages (from-to)178-181
Number of pages4
Issue number4836
StatePublished - 1988
Externally publishedYes

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme'. Together they form a unique fingerprint.

Cite this