A nutrient-dependent division antagonist is regulated post-translationally by the Clp proteases in Bacillus subtilis

Norbert S. Hill, Jason D. Zuke, P. J. Buske, An Chun Chien, Petra Anne Levin

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Background: Changes in nutrient availability have dramatic and well-defined impacts on both transcription and translation in bacterial cells. At the same time, the role of post-translational control in adaptation to nutrient-poor environments is poorly understood. Previous studies demonstrate the ability of the glucosyltransferase UgtP to influence cell size in response to nutrient availability. Under nutrient-rich medium, interactions with its substrate UDP-glucose promote interactions between UgtP and the tubulin-like cell division protein FtsZ in Bacillus subtilis, inhibiting maturation of the cytokinetic ring and increasing cell size. In nutrient-poor medium, reductions in UDP-glucose availability favor UgtP oligomerization, sequestering it from FtsZ and allowing division to occur at a smaller cell mass. Results: Intriguingly, in nutrient-poor conditions UgtP levels are reduced ∼ 3-fold independent of UDP-glucose. B. subtilis cells cultured under different nutrient conditions indicate that UgtP accumulation is controlled through a nutrient-dependent post-translational mechanism dependent on the Clp proteases. Notably, all three B. subtilis Clp chaperones appeared able to target UgtP for degradation during growth in nutrient-poor conditions. Conclusions: Together these findings highlight conditional proteolysis as a mechanism for bacterial adaptation to a rapidly changing nutritional landscape.

Original languageEnglish
Article number29
JournalBMC Microbiology
Volume18
Issue number1
DOIs
StatePublished - Apr 6 2018

Keywords

  • Cell cycle
  • Cell division
  • Cell size
  • ClpP
  • UDP-glucose
  • UgtP

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