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© Institut Pasteur
Structure de macromolécules : dimère d'aquométhémoglobine de cheval. Dérivé toxique oxydé de l'hémoglobine, représentant 1 à 2% du total.
Publication : FEBS letters

The FHA-containing protein GarA acts as a phosphorylation-dependent molecular switch in mycobacterial signaling

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 27 Dec 2008

England P, Wehenkel A, Martins S, Hoos S, André-Leroux G, Villarino A, Alzari PM

Link to Pubmed [PMID] – 19114043

FEBS Lett. 2009 Jan;583(2):301-7

Fork-head associated (FHA) domains are widely found in bacteria, but their cellular functions remain unclear. Here, we focus on Mycobacterium tuberculosis GarA, an FHA-containing protein conserved in actinomycetes that is phosphorylated by different Ser/Thr protein kinases. Using various physicochemical approaches, we show that phosphorylation significantly stabilizes GarA, and that its FHA domain interacts strongly with the phosphorylated N-terminal extension. Altogether, our results indicate that phosphorylation triggers an intra-molecular protein closure, blocking the phosphothreonine-binding site and switching off the regulatory properties of GarA. The model can explain the reported functions of this mycobacterial protein as regulator of glycogen degradation and glutamate metabolism.

http://www.ncbi.nlm.nih.gov/pubmed/19114043