E. coli RNAase P has a required RNA component in vivo

Ryszard Kole, Madeline F. Baer, Benjamin C. Stark, Sidney Altman

Research output: Contribution to journalArticle

88 Citations (Scopus)

Abstract

RNAase P has been partially purified from three thermosensitive strains of E. coli and the thermal inactivation characteristics of each preparation have been determined. The RNAase P preparations from two of these mutant strains, ts241 and ts709, and the wild-type strain have been separated into RNA and protein components. Various mixtures of the reconstituted components have been checked in vitro for complementation of their thermal sensitivity properties. The protein component of RNAase P from ts241 and the RNA component of RNAase P from ts709, respectively, account for the thermal sensitivity of the RNAase P from the two strains. The amount of the RNA component of RNAase P is lower in ts709 than in ts241 or the wild-type parent, 4273. RNAase P partially purified from a revertant of the third mutant strain, A49, which maps at or near the ts241 mutation, has an altered charge when compared to the RNAase P from the parent strain, BF265. We conclude that mutations which affect either the protein or RNA component of RNAase P can confer thermal sensitivity on the enzyme both in vivo and in vitro.

Original languageEnglish (US)
Pages (from-to)881-887
Number of pages7
JournalCell
Volume19
Issue number4
DOIs
StatePublished - 1980
Externally publishedYes

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Escherichia coli
Hot Temperature
RNA
Mutation
Proteins
Enzymes
In Vitro Techniques

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Medicine(all)

Cite this

E. coli RNAase P has a required RNA component in vivo. / Kole, Ryszard; Baer, Madeline F.; Stark, Benjamin C.; Altman, Sidney.

In: Cell, Vol. 19, No. 4, 1980, p. 881-887.

Research output: Contribution to journalArticle

Kole, Ryszard ; Baer, Madeline F. ; Stark, Benjamin C. ; Altman, Sidney. / E. coli RNAase P has a required RNA component in vivo. In: Cell. 1980 ; Vol. 19, No. 4. pp. 881-887.
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