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Nucleic Acids Res. 2014 Jan;42(2):1117-28. doi: 10.1093/nar/gkt874. Epub 2013 Sep 29.

cAMP protein kinase phosphorylates the Mos1 transposase and regulates its activity: evidences from mass spectrometry and biochemical analyses.

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Innovation Moléculaire Thérapeutique, EA 6306, UFR Sciences Pharmaceutiques, Parc Grandmont, Université François Rabelais, 37200 Tours, France, Centre de Biophysique Moléculaire, UPR 4301 CNRS, Rue Charles Sadron, 45071 Orléans, France, Laboratoire Universitaire de Biodiversité et Ecologie Microbienne, IUT de Quimper, Université de Bretagne Occidentale, 6 rue de l'Université, 29000 Quimper, France and Biologie Cellulaire de la Synapse, INSERM U789, Ecole Normale Supérieure, 46 rue d'Ulm, 75005 Paris, France.


Genomic plasticity mediated by transposable elements can have a dramatic impact on genome integrity. To minimize its genotoxic effects, it is tightly regulated either by intrinsic mechanisms (linked to the element itself) or by host-mediated mechanisms. Using mass spectrometry, we show here for the first time that MOS1, the transposase driving the mobility of the mariner Mos1 element, is phosphorylated. We also show that the transposition activity of MOS1 is downregulated by protein kinase AMP cyclic-dependent phosphorylation at S170, which renders the transposase unable to promote Mos1 transposition. One step in the transposition cycle, the assembly of the paired-end complex, is specifically inhibited. At the cellular level, we provide evidence that phosphorylation at S170 prevents the active transport of the transposase into the nucleus. Our data suggest that protein kinase AMP cyclic-dependent phosphorylation may play a double role in the early stages of genome invasion by mariner elements.

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