Affinity chromatography with an immobilized RNA enzyme

A. Vioque, S. Altman

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

M1 RNA, the catalytic subunit of Escherichia coli RNase P, has been covalently linked at its 3' terminus to agarose beads. Unlike M1 RNA, which is active in solution in the absence of the protein component (C5) of RNase P, the RNA linked to the beads is active only in the presence of C5 protein. Affinity chromatography of crude extracts of E. coli on a column prepared from the beads to which the RNA has been crosslinked results in the purification of C5 protein in a single step. The protein has been purified in this manner from cells that contain a plasmid, pINIIIR20, which includes the gene that codes for C5 protein. A 6-fold amplification of the expression of C5 protein is found in these cells after induction as compared to cells that do not harbor the plasmid.

Original languageEnglish (US)
Pages (from-to)5904-5908
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume83
Issue number16
DOIs
StatePublished - Jan 1 1986
Externally publishedYes

ASJC Scopus subject areas

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