Literature DB >> 31744883

A novel mechanism of ribonuclease regulation: GcvB and Hfq stabilize the mRNA that encodes RNase BN/Z during exponential phase.

Hua Chen1, Angelica Previero1, Murray P Deutscher2.   

Abstract

RNase BN, the Escherichia coli RNase Z family member, plays a limited role in tRNA metabolism, in contrast to most other organisms. However, RNase BN does act on 6S RNA, the global transcription regulator, degrading it in exponential-phase cells and maintaining it at low levels during this phase of growth. RNase BN levels decrease in stationary-phase cells, leading to elevation of 6S RNA and subsequent regulation of RNA polymerase. These findings were the first indication that RNase BN itself is growth phase-regulated. Here, we analyze the mechanism of this regulation of RNase BN. We find that RNase BN decreases in stationary phase because its mRNA becomes unstable, due primarily to its degradation by RNase E. However, in exponential-phase cells rbn mRNA is stabilized due to binding by the sRNA, GcvB, and the protein, Hfq, which reduce cleavage by RNase E. Because the amount of GcvB decreases in stationary phase, rbn mRNA is less protected and becomes increasingly unstable resulting in reduction in the amount of RNase BN. The small RNA-dependent, positive regulation of RNase BN in exponential-phase cells is the first example of this novel mechanism for RNase regulation.
© 2019 Chen et al.

Entities:  

Keywords:  RNA; bacteria; growth-phase regulation; mRNA decay; mRNA stability; post-transcriptional regulation; regulatory RNA; ribonuclease

Mesh:

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Year:  2019        PMID: 31744883      PMCID: PMC6937589          DOI: 10.1074/jbc.RA119.011367

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  45 in total

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Authors:  Murray P Deutscher
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2.  Growth Phase-dependent Variation of RNase BN/Z Affects Small RNAs: REGULATION OF 6S RNA.

Authors:  Hua Chen; Tanmay Dutta; Murray P Deutscher
Journal:  J Biol Chem       Date:  2016-11-08       Impact factor: 5.157

3.  Acetylation regulates the stability of a bacterial protein: growth stage-dependent modification of RNase R.

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10.  Reversible acetylation on Lys501 regulates the activity of RNase II.

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