Proteomics

Dataset Information

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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

Dataset's files

Source:
Action DRS
160318_BCG_Wt2_F1_3ul.raw Raw
160318_BCG_Wt2_F2_4ul.raw Raw
160318_BCG_Wt2_F4_4ul.raw Raw
160318_BCG_Wt3_F1_3ul.raw Raw
160318_BCG_Wt3_F2_4ul.raw Raw
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Publications

Identification of Novel Physiological Substrates of <i>Mycobacterium bovis</i> 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 <i>in vivo</i>, 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 <i>Mycobacterium bovis</i> BCG. The study compared the phosphoproteome dynamics during the b  ...[more]

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