Proteomics

Dataset Information

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The Mycobacterium tuberculosis O-phosphorylation landscape


ABSTRACT: LC-MS/MS tryptic peptide data comprising both label free (phosphoproteome) and TMT10 (global and phosphoproteome) analysis of mycobacterium tuberculosis mutants (WT, GoF, and LoF) grown at stationary phase. Data was searched with MS-GF+ (TMT) and MaxQuant (label free).

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive HF-X, Q Exactive Plus

ORGANISM(S): Mycobacterium Tuberculosis (ncbitaxon:1773)

SUBMITTER: Christoph Grundner  

PROVIDER: MSV000088254 | MassIVE | Thu Oct 21 23:56:00 BST 2021

SECONDARY ACCESSION(S): PXD029278

REPOSITORIES: MassIVE

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Publications

The Mycobacterium tuberculosis protein O-phosphorylation landscape.

Frando Andrew A   Boradia Vishant V   Gritsenko Marina M   Beltejar Claude C   Day Le L   Sherman David R DR   Ma Shuyi S   Jacobs Jon M JM   Grundner Christoph C  

Nature microbiology 20230123 3


Bacterial phosphosignalling has been synonymous with two-component systems and their histidine kinases, but many bacteria, including Mycobacterium tuberculosis (Mtb), also code for Ser/Thr protein kinases (STPKs). STPKs are the main phosphosignalling enzymes in eukaryotes but the full extent of phosphorylation on protein Ser/Thr and Tyr (O-phosphorylation) in bacteria is untested. Here we explored the global signalling capacity of the STPKs in Mtb using a panel of STPK loss-of-function and overe  ...[more]

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