Properties of purified ribonuclease P from Escherichia coli

Ryszard Kole, Sidney Altman

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

The purified protein moiety of ribonuclease P (EC 3.1.26.5) from Escherichia coli, a single polypeptide of molecular weight ∼17 500, has no catalytic activity by itself on several RNA substrates. However, when it is mixed in vitro with an RNA species called M1 RNA, RNase P activity is reconstituted. The rate at which the purified RNase P cleaves any particular tRNA precursor molecule depends on the identity of that tRNA precursor.

Original languageEnglish (US)
Pages (from-to)1902-1906
Number of pages5
JournalBiochemistry
Volume20
Issue number7
StatePublished - 1981
Externally publishedYes

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Ribonuclease P
Escherichia coli
RNA Precursors
RNA
Catalyst activity
Molecular Weight
Molecular weight
Peptides
Molecules
Substrates
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Properties of purified ribonuclease P from Escherichia coli. / Kole, Ryszard; Altman, Sidney.

In: Biochemistry, Vol. 20, No. 7, 1981, p. 1902-1906.

Research output: Contribution to journalArticle

Kole, Ryszard ; Altman, Sidney. / Properties of purified ribonuclease P from Escherichia coli. In: Biochemistry. 1981 ; Vol. 20, No. 7. pp. 1902-1906.
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