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SsrA-mediated tagging in Bacillus subtilis.

T Wiegert¹, W Schumann

¹Institute of Genetics, University of Bayreuth, D-95440 Bayreuth, Germany.

Journal of Bacteriology

|June 8, 2001

Summary

Bacteria use tmRNA to tag and degrade stalled proteins. In Bacillus subtilis, this process involves the ssrA gene and targets proteins for degradation by the ClpXP protease, primarily ClpP.

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Area of Science:

Molecular Biology
Bacterial Protein Degradation
Ribosome Rescue Mechanisms

Background:

Bacteria possess a tmRNA (encoded by ssrA) system to rescue stalled ribosomes.
This system adds a proteolytic tag to truncated proteins, targeting them for degradation.
Understanding this mechanism is crucial for bacterial protein homeostasis.

Purpose of the Study:

To investigate the ssrA-mediated protein tagging and degradation in Bacillus subtilis.
To identify the specific proteases responsible for degrading SsrA-tagged proteins in B. subtilis.

Main Methods:

Constructed a bipartite detection system using HrcA repressor and bgaB reporter gene.
Fused the proteolytic tag to HrcA and manipulated its stop codon and tag sequence.
Utilized ssrA and smpB gene inactivation and tested protease-deficient B. subtilis strains.

Main Results:

Tagged HrcA showed constitutive high-level beta-galactosidase expression due to instability.
Modifications to the tag's C-terminal residues or stop codon affected HrcA stability.
Inactivation of ssrA or smpB prevented tagging; HrcA remained stable only in clpX/clpP mutants.

Conclusions:

The ssrA-mediated trans-translation tagging is essential for HrcA degradation in B. subtilis.
The ClpXP ATP-dependent protease, particularly ClpP, is the primary enzyme for degrading SsrA-tagged proteins.
This study elucidates the key players in bacterial ribosome rescue and protein turnover.

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