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Related Experiment Videos

Associations between Bacillus subtilis sigmaB regulators in cell extracts.

Shrin Kuo1, Shuyu Zhang, Robyn L Woodbury

  • 1Department of Microbiology and Immunology, University of Texas Health Science Center, San Antonio, TX 78229-3900, USA.

Microbiology (Reading, England)
|December 8, 2004
PubMed
Summary

Bacillus subtilis stress response involves RsbR/RsbS complexes, but RsbT does not stably bind them. Ribosomes and Obg do not form stable associations with the Rsb complex, suggesting RsbT

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • The Bacillus subtilis general stress regulon is activated by sigma(B) transcription factor.
  • Sigma(B) activation follows dephosphorylation of its regulator RsbV by phosphatases responding to physical or nutritional stress.
  • Physical stress phosphatase (RsbU) activity requires RsbT, which is released from an inhibitory complex (RsbR/RsbS) upon stress signaling.

Purpose of the Study:

  • Investigate the associations between RsbR, RsbS, RsbT, Obg, and ribosomes in Bacillus subtilis.
  • Determine the basis for coelution of these proteins in high-molecular-mass fractions.
  • Clarify the role of RsbR paralogs and ribosome-associated proteins in RsbT complex formation and stress response.

Main Methods:

  • Analysis of protein-protein interactions in wild-type and mutant B. subtilis extracts.

Related Experiment Videos

  • Expression and analysis of RsbR, RsbS, and RsbT in engineered Escherichia coli.
  • Gel-filtration chromatography and Triton solubility assays.

    • Main Results:

    • Large RsbR/RsbS complexes, independent of ribosomes, were detected in both B. subtilis and E. coli.
    • RsbR paralogs in B. subtilis can substitute for RsbR in complex formation.
    • RsbT did not stably associate with RsbR/RsbS complexes; high-molecular-mass RsbT likely represents Triton-sensitive aggregates.
    • Ribosomes/Obg do not form stable associations with the Rsb complex.

    Conclusions:

    • The RsbR/RsbS complex formation is conserved across B. subtilis and E. coli, with B. subtilis paralogs contributing.
    • RsbT's lack of stable binding to the RsbR/RsbS complex and its aggregation suggest inherent instability.
    • The stress-derived signal for RsbT release remains unknown, but stable association with ribosomes/Obg is not involved.