The Mycobacterium tuberculosis GroEL1 chaperone is a substrate of Ser/Thr protein kinases.
We demonstrate that Mycobacterium tuberculosis GroEL1 is phosphorylated by PknF at two positions, Thr25 and Thr54. Unexpectedly, Mycobacterium smegmatis GroEL1 is not a substrate of its cognate PknF. This study shows that the phosphorylation profiles of conserved proteins are species dependent and provide insights that may explain the numerous biological functions of these important proteins.
Canova
Marc J
MJ
Institut de Biologie et Chimie des Protéines (IBCP UMR 5086), CNRS, Université Lyon 1, IFR128 BioSciences, Lyon-Gerland, 7 passage du Vercors, 69367 Lyon Cedex 07, France. vmolle@ibcp.fr
Kremer
Laurent
L
Molle
Virginie
V
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D018834:Chaperonin 60 / Q000378:metabolism*; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000502:physiology*; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D016415:Sequence Alignment; D013912:Threonine / Q000378:metabolism
D001426:Bacterial Proteins; D018834:Chaperonin 60; D013912:Threonine; C487814:PknF protein, Mycobacterium tuberculosis; D017346:Protein Serine-Threonine Kinases