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Bouchet N., Jaillet J., Gabant G., Brillet B., Briseno Roa L., Cadene M. and Augé-Gouillou C.

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

Nucleic Acids Research 42 (2) 1117-1128 - doi : 10.1093/nar/gkt874

par Frapart - publié le , mis à jour le

Abstract :

Genomic plasticity mediated by transposable elements can have a dramatic impact on genome integrity. In order 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 down regulated by PKA 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 PKA phosphorylation may play a double role in the early stages of genome invasion by mariner elements.