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A novel mechanism of ribonuclease regulation: GcvB and Hfq stabilize the mRNA that encodes RNase BN/Z during exponential phase
- Source :
- J Biol Chem
- Publication Year :
- 2019
-
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.
- Subjects :
- 0301 basic medicine
RNase P
RNA Stability
Host Factor 1 Protein
Cleavage (embryo)
Biochemistry
03 medical and health sciences
chemistry.chemical_compound
RNA polymerase
Endoribonucleases
Escherichia coli
Ribonuclease
RNA, Messenger
Molecular Biology
Post-transcriptional regulation
Messenger RNA
030102 biochemistry & molecular biology
biology
Base Sequence
Escherichia coli Proteins
RNA
Cell Biology
Cell biology
030104 developmental biology
chemistry
Transfer RNA
Exoribonucleases
biology.protein
RNA, Small Untranslated
Transcription Initiation Site
Protein Binding
Subjects
Details
- ISSN :
- 1083351X
- Volume :
- 294
- Issue :
- 52
- Database :
- OpenAIRE
- Journal :
- The Journal of biological chemistry
- Accession number :
- edsair.doi.dedup.....653ae047b07efdfef0409a4d5cf4d93b