The Mycobacterium tuberculosis GroEL1 Chaperone Is a Substrate of Ser/Thr Protein Kinases ▿
- 1Institut 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
- 2Laboratoire de Dynamique des Interactions Membranaires Normales et Pathologiques, Universités de Montpellier II et I, CNRS 5235, case 107, Place Eugène Bataillon, 34095 Montpellier Cedex 05, France
- 3INSERM, DIMNP, Place Eugène Bataillon, 34095 Montpellier Cedex 05, France
ABSTRACT
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.
FOOTNOTES
- Received 4 November 2008.
- Accepted 30 January 2009.
- *Corresponding author. Mailing address for Virginie Molle: 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. Phone: (33) 4 72 72 26 79. Fax: (33) 4 72 72 26 41. E-mail: vmolle{at}ibcp.fr. Mailing address for Laurent Kremer: Laboratoire de Dynamique des Interactions Membranaires Normales et Pathologiques, Universités de Montpellier II et I, CNRS 5235, case 107, Place Eugène Bataillon, 34095 Montpellier Cedex 05, France. Phone: (33) 4 67 14 33 81. Fax: (33) 4 67 14 42 86. E-mail: laurent.kremer{at}univ-montp2.fr
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↵▿ Published ahead of print on 6 February 2009.
- American Society for Microbiology
