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Background  Sensing and responding to environmental changes is a central aspect of cell division regulation.  Mycobacterium tuberculosis  contains eleven Ser/Thr kinases, two of which, PknA and PknB, are key signaling molecules that regulate cell division/morphology. One substrate of these kinases is Wag31, and we previously showed that partial depletion of Wag31 caused morphological changes indicative of cell wall defects, and that the phosphorylation state of Wag31 affected cell growth in mycobacteria. In the present study, we further characterized the role of the Wag31 phosphorylation in polar peptidoglycan biosynthesis.    Results  We demonstrate that the differential growth among cells expressing different  wag31  alleles (wild-type, phosphoablative, or phosphomimetic) is caused by, at least in part, dissimilar nascent peptidoglycan biosynthesis. The phosphorylation state of Wag31 is found to be important for protein-protein interactions between the Wag31 molecules, and thus, for its polar localization. Consistent with these results, cells expressing a phosphomimetic  wag31  allele have a higher enzymatic activity in the peptidoglycan biosynthetic pathway.    Conclusions  The Wag31 Mtb  phosphorylation is a novel molecular mechanism by which Wag31 Mtb  regulates peptidoglycan synthesis and thus, optimal growth in mycobacteria.

Regulation of Polar Peptidoglycan Biosynthesis by Wag31 Phosphorylation in Mycobacteria