Effect of Wag31 phosphorylation on nascent peptidoglycan biosynthesis

This study demonstrated that Wag31Mtb phosphorylation, which is unique among DivIVA homologues, regulates polar peptidoglycan biosynthesis and optimal growth of mycobacterial cells through modulating the localization of Wag31 and the activity of peptidoglycan biosynthetic enzymes.

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25/08/2010 · Regulation of Polar Peptidoglycan Biosynthesis by Wag31 ..
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In the present report, we further characterize the role of Wag31 phosphorylation. We show that the differential growth caused by the expression of different wag31Mtb alleles (wild-type wag31Mtb, wag31T73AMtb, and wag31T73EMtb) is due to, at least in part, dissimilar nascent peptidoglycan biosynthesis. We further show that the phosphorylation state of Wag31 is important for protein-protein interaction between the Wag31Mtb molecules, and thus, for its polar localization. In line with these findings, we observe a higher enzymatic activity (MraY and MurG) of peptidoglycan biosynthetic pathway in cells expressing phosphomimetic wag31T73EMtb than cells expressing wild-type wag31Mtb or phosphoablative wag31T73AMtb.

Biosynthesis of the Peptidoglycan of Bacterial Cell Walls

To further confirm the effect of the Wag31 phosphorylation on its polar localization, we examined the localization of wild-type Wag31Mtb in the presence or absence of pknAMtb- or pknBMtb-overexpression. We previously showed that Wag31 was weakly phosphorylated by PknAMtb, which was significantly enhanced by the addition of PknBMtb in vitro []. Consistent with this, pknA-overexpression only slightly increased the polar localization of Wag31 and polar peptidoglycan biosynthesis (Additional file (Fig. A2)). However, overexpression of pknBMtb, which dramatically increased the phosphorylation of GFP-Wag31 (Figure bottom panel), elevated the polar localization of Wag31 (two-fold, upper panel) and nascent peptidoglycan biosynthesis (1.8-fold, middle panel) compared to cells without pknBMtb-overexpression. These data further support that the phosphorylation of Wag31 enhances its polar localization, which in turn heightens polar peptidoglycan biosynthesis.

25/12/2015 · Biosynthesis of the Peptidoglycan of Bacterial Cell Walls III
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PEPTIDOGLYCAN STRUCTURE AND COMPOSITION ..

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.

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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.

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Fig. A2: Localization of Wag31 and nascent peptidoglycan biosynthesis in the presence or absence of pknAMtb-overexpression. Examination of wild-type Wag31 localization and polar peptidoglycan biosynthesis when pknA is overexpressed in M. smegmatis.