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

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.