The ClpY-ClpQ protease regulates multicellular development in Bacillus subtilis
| العنوان: | The ClpY-ClpQ protease regulates multicellular development in Bacillus subtilis |
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| المؤلفون: | Jian-Hua Guo, Yiyang Yu, Yunrong Chai, Yun Chen, Yuxuan Qin, Fang Yan, Yinghao He |
| المصدر: | Microbiology. 164:848-862 |
| بيانات النشر: | Microbiology Society, 2018. |
| سنة النشر: | 2018 |
| مصطلحات موضوعية: | Proteomics, 0301 basic medicine, Proteases, Operon, medicine.medical_treatment, 030106 microbiology, Mutant, Swarming motility, HslVU, Bacillus subtilis, Microbiology, 03 medical and health sciences, Bacterial Proteins, medicine, Protease, biology, Extracellular Polymeric Substance Matrix, Chemistry, Biofilm, Endopeptidase Clp, Gene Expression Regulation, Bacterial, biology.organism_classification, Cell biology, Polyglutamic Acid, Biofilms, Trans-Activators, biology.protein, Gene Deletion, Locomotion, Flagellin |
| الوصف: | 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 Bacillus subtilis, the ΔclpYQ deletion mutant formed early and robust biofilms, while swarming motility was severely impaired. Colonies of the ΔclpYQ mutant were also much less mucoid on agar plates, indicating the loss of the production of secreted γ-poly-dl-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 ΔclpYQ mutant. The results from both iTRAQ and Western immunoblotting showed that levels of the biofilm master repressor SinR were modestly reduced in the ΔclpYQ 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 clpYQ in the same operon, was not impacted on by ΔclpYQ. Lastly, our results suggested that, unlike in Escherichia coli, ClpYQ does not play an essential role in heat-shock response in both B. subtilis and Bacillus cereus. In conclusion, we propose that the ClpYQ protease is primarily involved in multicellular development in B. subtilis. |
| تدمد: | 1465-2080 1350-0872 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a481adce2e55116dafd158363f3e906b https://doi.org/10.1099/mic.0.000658 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....a481adce2e55116dafd158363f3e906b |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14652080 13500872 |
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