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• W2891069378 abstract "Tuberculosis claims >1 million lives annually, and its causative agent Mycobacterium tuberculosis is a highly successful pathogen. Protein kinase B (PknB) is reported to be critical for mycobacterial growth. Here, we demonstrate that PknB-depleted M. tuberculosis can replicate normally and can synthesize peptidoglycan in an osmoprotective medium. Comparative phosphoproteomics of PknB-producing and PknB-depleted mycobacteria identify CwlM, an essential regulator of peptidoglycan synthesis, as a major PknB substrate. Our complementation studies of a cwlM mutant of M. tuberculosis support CwlM phosphorylation as a likely molecular basis for PknB being essential for mycobacterial growth. We demonstrate that growing mycobacteria produce two forms of CwlM: a non-phosphorylated membrane-associated form and a PknB-phosphorylated cytoplasmic form. Furthermore, we show that the partner proteins for the phosphorylated and non-phosphorylated forms of CwlM are FhaA, a fork head-associated domain protein, and MurJ, a proposed lipid II flippase, respectively. From our results, we propose a model in which CwlM potentially regulates both the biosynthesis of peptidoglycan precursors and their transport across the cytoplasmic membrane." @default.
• W2891069378 created "2018-09-27" @default.
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• W2891069378 date "2018-10-01" @default.
• W2891069378 modified "2023-10-17" @default.
• W2891069378 title "Two Faces of CwlM, an Essential PknB Substrate, in Mycobacterium tuberculosis" @default.
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• W2891069378 doi "https://doi.org/10.1016/j.celrep.2018.09.004" @default.
• W2891069378 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6180346" @default.
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