A regulatory pathway that selectively up-regulates elongasome function in the absence of class A PBPs
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- Yesha Patel
- Department of Microbiology, Cornell University, Ithaca, United States
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- Heng Zhao
- Department of Microbiology, Cornell University, Ithaca, United States
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- John D Helmann
- Department of Microbiology, Cornell University, Ithaca, United States
書誌事項
- 公開日
- 2020-09-08
- 権利情報
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- http://creativecommons.org/licenses/by/4.0/
- http://creativecommons.org/licenses/by/4.0/
- http://creativecommons.org/licenses/by/4.0/
- DOI
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- 10.7554/elife.57902
- 公開者
- eLife Sciences Publications, Ltd
説明
<jats:p> Bacteria surround themselves with peptidoglycan, an adaptable enclosure that contributes to cell shape and stability. Peptidoglycan assembly relies on penicillin-binding proteins (PBPs) acting in concert with SEDS-family transglycosylases RodA and FtsW, which support cell elongation and division respectively. In <jats:italic>Bacillus subtilis</jats:italic> , cells lacking all four PBPs with transglycosylase activity (aPBPs) are viable. Here, we show that the alternative sigma factor σ <jats:sup>I</jats:sup> is essential in the absence of aPBPs. Defects in aPBP-dependent wall synthesis are compensated by σ <jats:sup>I</jats:sup> -dependent upregulation of an MreB homolog, MreBH, which localizes the LytE autolysin to the RodA-containing elongasome complex. Suppressor analysis reveals that cells unable to activate this σ <jats:sup>I</jats:sup> stress response acquire gain-of-function mutations in the essential histidine kinase WalK, which also elevates expression of <jats:italic>sigI</jats:italic> , <jats:italic>mreBH</jats:italic> and <jats:italic>lytE</jats:italic> . These results reveal compensatory mechanisms that balance the directional peptidoglycan synthesis arising from the elongasome complex with the more diffusive action of aPBPs. </jats:p>
収録刊行物
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- eLife
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eLife 9 2020-09-08
eLife Sciences Publications, Ltd
