RNases and Helicases in Gram-Positive Bacteria.

Microbiol Spectr

UMR8261 CNRS, Université Paris Diderot (Sorbonne Paris Cité), Institut de Biologie Physico-Chimique, Paris, France.

Published: April 2018

AI Article Synopsis

  • RNases are crucial enzymes for RNA processing and breakdown in all life forms, but each group (bacteria, archaea, eukaryotes) has developed unique RNase sets.
  • Bacteria utilize RNases to adapt gene expression based on environmental changes, with over 20 distinct RNases identified in Gram-negative and Gram-positive bacteria, though many are not shared between the two.
  • The review focuses on key RNases in Gram-positive bacteria, especially RNase J1, RNase III, and RNase Y, and highlights how other proteins like helicases influence their RNA-degradation functions.

Article Abstract

RNases are key enzymes involved in RNA maturation and degradation. Although they play a crucial role in all domains of life, bacteria, archaea, and eukaryotes have evolved with their own sets of RNases and proteins modulating their activities. In bacteria, these enzymes allow modulation of gene expression to adapt to rapidly changing environments. Today, >20 RNases have been identified in both and , the paradigms of the Gram-negative and Gram-positive bacteria, respectively. However, only a handful of these enzymes are common to these two organisms and some of them are essential to only one. Moreover, although sets of RNases can be very similar in closely related bacteria such as the and , the relative importance of individual enzymes in posttranscriptional regulation in these organisms varies. In this review, we detail the role of the main RNases involved in RNA maturation and degradation in Gram-positive bacteria, with an emphasis on the roles of RNase J1, RNase III, and RNase Y. We also discuss how other proteins such as helicases can modulate the RNA-degradation activities of these enzymes.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11633581PMC
http://dx.doi.org/10.1128/microbiolspec.RWR-0003-2017DOI Listing

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