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Escherichia coli RNase E can efficiently replace RNase Y in Bacillus subtilis.

Soumaya Laalami1, Marina Cavaiuolo1, Sylvain Roque1

  • 1CNRS, UMR8261, Institut de Biologie Physico-Chimique, Université de Paris, 75005 Paris, France.

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RNase E from E. coli can functionally replace RNase Y in B. subtilis, restoring growth and global transcript profiles. Inner membrane localization of RNase E is crucial for this complementation, suggesting convergent evolution of these essential bacterial enzymes.

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Area of Science:

  • Bacterial molecular biology
  • Enzyme function and evolution
  • RNA processing and degradation

Background:

  • RNase Y and RNase E are essential endoribonucleases controlling mRNA turnover in Bacillus subtilis and Escherichia coli, respectively.
  • These enzymes share similar in vitro cleavage specificity and subcellular localization, hinting at potential functional overlap.

Purpose of the Study:

  • To investigate the functional equivalence of RNase E and RNase Y in vivo by assessing RNase E's ability to complement RNase Y-deficient B. subtilis.
  • To identify key features of RNase E, such as localization and domain structure, critical for functional complementation.

Main Methods:

  • Genetic complementation experiments introducing full-length and truncated RNase E into an RNase Y mutant of B. subtilis.
  • Analysis of bacterial growth rates and genome-wide transcript profiling using high-throughput sequencing.
  • In vitro cleavage assays comparing RNase Y, E, and J activities.

Main Results:

  • Full-length RNase E significantly restored wild-type growth in the B. subtilis rny mutant.
  • RNase E expression reversed transcript profiles at both individual gene and genome-wide levels.
  • Inner membrane localization of RNase E was essential for efficient complementation, while C-terminal truncations had minor effects.

Conclusions:

  • RNase E can functionally substitute for RNase Y in B. subtilis, demonstrating significant in vivo functional equivalence.
  • Subcellular localization, specifically inner membrane targeting, is a critical determinant for the biological function of these essential bacterial ribonucleases.
  • RNase Y and RNase E exemplify convergent evolution, developing similar low-specificity endonuclease activities vital for bacterial mRNA metabolism.