New substrates and interactors of the mycobacterial Serine/Threonine protein kinase PknG identified by a tailored interactomic approach

PknG from Mycobacterium tuberculosis is a multidomain Serine/Threonine protein kinase that regulates bacterial metabolism as well as the pathogen's ability to survive inside the host by still uncertain mechanisms. To uncover PknG interactome we developed an affinity purification-mass spectromet...

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Detalles Bibliográficos
Autores principales: Gil, M., Lima, A., Rivera, B., Rossello, J., Urdániz, E., Cascioferro, A., Carrión, F., Wehenkel, A., Bellinzoni, M., Batthyány, C., Pritsch, O., Denicola, A., Alvarez, M.N., Carvalho, P.C., Lisa, M.-N., Brosch, R., Piuri, M., Alzari, P.M., Durán, R.
Formato: JOUR
Materias:
Affinity purification-mass spectrometry
FhaA
glutamine synthetase
Mycobacterium tuberculosis
PknG
Serine/Threonine protein kinase
50s ribosomal protein L13
60 kda chaperonin 1
acetyl propionyl coenzyme A carboxylase alpha chain
alcohol dehydrogenase iron containing protein
bacterial enzyme
fhaa protein
gara protein
glutamate ammonia ligase
inorganic pyrophosphatase
pkng protein
protein DnaK
protein serine threonine kinase
unclassified drug
affinity chromatography
Article
autophosphorylation
bacterial cell wall
bacterial strain
controlled study
enzyme analysis
enzyme phosphorylation
enzyme purification
enzyme substrate
ferredoxin iron sulfur binding protein
in vitro study
mass spectrometry
molecular docking
nitrogen fixation
nonhuman
priority journal
translation regulation
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_18743919_v192_n_p321_Gil
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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