Characterization of the RNase R association with ribosomes

BMC Microbiol. 2014 Feb 11:14:34. doi: 10.1186/1471-2180-14-34.

Abstract

Background: In this study we employed the TAP tag purification method coupled with mass spectrometry analysis to identify proteins that co-purify with Escherichia coli RNase R during exponential growth and after temperature downshift.

Results: Our initial results suggested that RNase R can interact with bacterial ribosomes. We subsequently confirmed this result using sucrose gradient ribosome profiling joined with western blot analysis. We found that RNase R co-migrates with the single 30S ribosomal subunits. Independent data involving RNase R in the rRNA quality control process allowed us to hypothesize that the RNase R connection with ribosomes has an important physiological role.

Conclusions: This study leads us to conclude that RNase R can interact with ribosomal proteins and that this interaction may be a result of this enzyme involvement in the ribosome quality control.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Centrifugation, Density Gradient
  • Escherichia coli / enzymology*
  • Escherichia coli / growth & development
  • Escherichia coli / metabolism*
  • Escherichia coli / radiation effects
  • Escherichia coli Proteins / metabolism*
  • Exoribonucleases / metabolism*
  • Protein Binding
  • Ribosomes / metabolism*
  • Temperature

Substances

  • Escherichia coli Proteins
  • rnr protein, E coli
  • Exoribonucleases