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Volume 164, Issue 5

The ClpY-ClpQ protease regulates multicellular development in Free

Abstract

ATP-dependent proteases play essential roles in both protein quality control and the regulation of protein activities in bacteria. ClpYQ (also known as HslVU) is one of several highly conserved ATP-dependent proteases in bacteria. The regulation and biological function of ClpYQ have been well studied in Gram-negative bacteria, but are poorly understood in Gram-positive species. In this study, we showed that in the Gram-positive bacterium the Δ deletion mutant formed early and robust biofilms, while swarming motility was severely impaired. Colonies of the Δ mutant were also much less mucoid on agar plates, indicating the loss of the production of secreted γ-poly--glutamic acid (γ-PGA). Global proteomic analysis using isobaric tags for relative and absolute quantification (iTRAQ) confirmed that a number of proteins involved in motility, chemotaxis and the production of γ-PGA were less abundant in the Δ mutant. The results from both iTRAQ and Western immunoblotting showed that levels of the biofilm master repressor SinR were modestly reduced in the Δ mutant, but probably significantly enough to alter biofilm regulation due to the ultrasensitivity of the expression of biofilm genes to SinR protein levels. Western immunoblotting also showed that the abundance of CodY, whose gene is clustered with in the same operon, was not impacted on by Δ. Lastly, our results suggested that, unlike in , ClpYQ does not play an essential role in heat-shock response in both and . In conclusion, we propose that the ClpYQ protease is primarily involved in multicellular development in .

  • Received:
  • Accepted:
  • Published Online:
Keyword(s): Bacillus subtilis , biofilm formation , ClpYQ , HslVU , ITRAQ and motility
© 2018 The Authors
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2018-05-01
2024-04-25
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The ClpY-ClpQ protease regulates multicellular development in Bacillus subtilis
Microbiology 164, 848 (2018); https://doi.org/10.1099/mic.0.000658
/content/journal/micro/10.1099/mic.0.000658
/content/journal/micro/10.1099/mic.0.000658
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