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M. bovis BCG PknG physiological substrates

ABSTRACT: Mycobacterial Ser/Thr kinases play a critical role in bacterial physiology and pathogenesis. Linking kinases to the substrates they phosphorylate in vivo, thereby elucidating their exact functions, is still a challenge. The aim of this work was to associate protein phosphorylation in mycobacteria with important subsequent macro cellular events by identifying the physiological substrates of PknG in Mycobacterium bovis BCG. The study compared the phosphoproteome dynamics during the batch growth of M. bovis BGC versus the respective PknG knock-out mutant (ΔPknG-BCG) strains.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mycobacterium Bovis Bcg Str. Pasteur 1173p2

DISEASE(S): Tuberculosis

SUBMITTER: Kehilwe Nakedi

LAB HEAD: Jonathan M Blackburn

PROVIDER: PXD006473 | Pride | 2018-03-23

REPOSITORIES: Pride

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Identification of Novel Physiological Substrates of Mycobacterium bovis BCG Protein Kinase G (PknG) by Label-free Quantitative Phosphoproteomics.

Nakedi Kehilwe C KC Calder Bridget B Banerjee Mousumi M Giddey Alexander A Nel Andrew J M AJM Garnett Shaun S Blackburn Jonathan M JM Soares Nelson C NC

Molecular & cellular proteomics : MCP 20180316 7

Mycobacterial Ser/Thr kinases play a critical role in bacterial physiology and pathogenesis. Linking kinases to the substrates they phosphorylate in vivo, thereby elucidating their exact functions, is still a challenge. The aim of this work was to associate protein phosphorylation in mycobacteria with important subsequent macro cellular events by identifying the physiological substrates of PknG in Mycobacterium bovis BCG. The study compared the phosphoproteome dynamics during the b ...[more]

PMID: 29549130

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