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Updated: Jun 17, 2026
08:58
In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
Published on: September 2, 2019
Bacillus subtilis ribonucleases J1 and J2 form a complex with altered enzyme behaviour
Nathalie Mathy1, Agnès Hébert, Peggy Mervelet
1CNRS UPR 9073 (affiliated with Université de Paris 7-Denis Diderot), Paris, France.
Molecular Microbiology
|December 23, 2009
Summary
Newly discovered ribonucleases J1 and J2 in Bacillus subtilis form a complex, altering RNA processing. This RNase J1/J2 complex reveals synergistic activity, changing how these essential enzymes function.
Area of Science:
- Molecular Biology
- Enzymology
- RNA Metabolism
Background:
- Ribonucleases J1 and J2 are essential enzymes in Bacillus subtilis, involved in RNA maturation and degradation.
- These enzymes possess both 5'-to-3' exoribonucleolytic and endoribonucleolytic activities.
- Previously, RNase J1 and J2 were thought to function independently.
Purpose of the Study:
- To investigate the functional relationship between Ribonucleases J1 and J2.
- To determine if RNase J1 and J2 interact or form a complex.
- To characterize the enzymatic activities of individual RNases and their complex.
Main Methods:
- Biochemical assays to measure exoribonuclease and endoribonuclease activities.
- Analysis of enzyme kinetics and cleavage site specificities.
- In vitro studies using purified RNase J1, RNase J2, and a combined RNase J1/J2 preparation.
Main Results:
- Evidence suggests RNases J1 and J2 form a complex, likely the predominant form in vivo.
- The RNase J1/J2 complex exhibits robust 5'-to-3' exoribonuclease activity, primarily driven by RNase J1.
- Complex formation synergistically alters endoribonucleolytic cleavage site preference and efficiency.
Conclusions:
- RNase J1 and J2 function as a complex, not independently, significantly impacting RNA processing.
- The essentiality of RNase J1 may be linked to its dominant exoribonuclease activity within the complex.
- This study provides insights into enzyme subfunctionalization following gene duplication and novel mechanisms of RNA regulation.
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