An immunological determinant of RNase P protein is conserved between Escherichia coli and humans

M. J. Mamula, M. Baer, J. Craft, S. Altman

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

RNase P, an enzyme with RNA and protein subunits, cleaves tRNA precursor molecules to form the 5' termini of mature tRNAs in both prokaryotes and eukaryotes. Rabbit antibodies made against the protein subunit, C5 protein, of Escherichia coli RNase P bound RNase P protein from E. coli and Bacillus subtilis in immunoblots and solid-phase immunoassays. These rabbit anti-C5 antibodies also bound a protein (M(r)) ~ 40,000) in preparations of RNase P from human (HeLa) cells and depleted the enzymatic activity from preparations of RNase P from both human and E. coli cells. Finally, rabbit anti-C5 antibodies immunoprecipitated from crude extracts of human cells a ribonucleoprotein complex containing H1 RNA, the putative RNA component of human RNase P. These results show that an antigenic determinant is shared by C5 protein from E. coli RNase P and a protein component of RNase P from human cells.

Original languageEnglish (US)
Pages (from-to)8717-8721
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume86
Issue number22
DOIs
StatePublished - Dec 14 1989
Externally publishedYes

Keywords

  • epitope
  • ribonucleoprotein
  • tRNA processing

ASJC Scopus subject areas

  • General

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