Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification
2016
Stanger, Frédééric V. | Burmann, Bjorn M. | Harms, Alexander | Aragééão, Hugo | Mazur, Adam | Sharpe, Timothy | Dehio, Christoph | Hiller, J. Sabastian (John Sabastian) | Schirmer, Tilman
Significance FIC-domain enzymes are found in all kingdoms of life and catalyze posttranslational modifications of various target proteins to modulate their function. Because the vast majority of Fic proteins are expressed in an inhibited form, their physiological importance has escaped attention for a long time. This article reveals an autonomous mechanism of inhibition relief for class III Fic proteins, which hinges on autoadenylylation of an inhibitory helix. Because the process occurs in cis , the Fic enzyme constitutes a molecular timer that operates independent of enzyme concentration. Furthermore, we show that Fic-mediated adenylylation of DNA gyrase leads to bacterial growth arrest. Thus, the time-dependent inactivation of DNA gyrase may serve as a switch to bacterial dormancy under starvation or other stress conditions.
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