Proteins associated with RNase E in a multicomponent ribonucleolytic complex

Andras Miczak, Vladimir R. Kaberdin, Chia Li Wei, Sue Lin-Chao

Research output: Contribution to journalArticle

301 Citations (Scopus)

Abstract

The Escherichia coli endoribonuclease RNase E is essential for RNA processing and degradation. Earlier work provided evidence that RNase E exists intracellularly as part of a multicomponent complex and that one of the components of this complex is a 3'-to-5' exoribonuclease, polynucleotide phosphorylase (EC 2.7.7.8). To isolate and identify other components of the RNase E complex, FLAG-epitope-tagged RNase E (FLAG-Rne) fusion protein was purified on a monoclonal antibody-conjugated agarose column. The FLAG-Rne fusion protein, eluted by competition with the synthetic FLAG peptide, was found to be associated with other proteins. N-terminal sequencing of these proteins revealed the presence in the RNase E complex not only of polynucleotide phosphorylase but also of DnaK, RNA helicase, and enolase (EC 4.2.1.11). Another protein associated only with epitope-tagged temperature- sensitive (Rne-3071) mutant RNase E but not with the wild-type enzyme is GroEL. The FLAG-Rne complex has RNase E activity in vivo and in vitro. The relative amount of proteins associated with wild-type and Rne-3071 expressed at an elevated temperature differed.

Original languageEnglish
Pages (from-to)3865-3869
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume93
Issue number9
DOIs
Publication statusPublished - Apr 30 1996

Keywords

  • DnaK
  • RNA helicase
  • enolase

ASJC Scopus subject areas

  • General

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