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

BMC Microbiology

Norbert S. Hill¹  P. J. Buske²  Jason D. Zuke³ 

[1] Department of Biology, Washington University, St. Louis, USA;Present address: Department of Bacteriology, University of Wisconsin, Madison, USA;Present address: Department of Molecular and Cell Biology, University of California, Berkeley, USA

关键词: Cell cycle;    Cell size;    Cell division;    ClpP;    UgtP;    UDP-glucose;   

DOI  :  10.1186/s12866-018-1155-2

学科分类：微生物学和免疫学

来源: BioMed Central

【 摘 要 】

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. 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. Together these findings highlight conditional proteolysis as a mechanism for bacterial adaptation to a rapidly changing nutritional landscape.

【 授权许可】

CC BY