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

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...

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Autores principales: Bouchet, Nicolas, Jaillet, Jérôme, Gabant, Guillaume, Brillet, Benjamin, Briseño-Roa, Luis, Cadene, Martine, Augé-Gouillou, Corinne
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3902898/
https://www.ncbi.nlm.nih.gov/pubmed/24081583
http://dx.doi.org/10.1093/nar/gkt874
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author Bouchet, Nicolas
Jaillet, Jérôme
Gabant, Guillaume
Brillet, Benjamin
Briseño-Roa, Luis
Cadene, Martine
Augé-Gouillou, Corinne
author_facet Bouchet, Nicolas
Jaillet, Jérôme
Gabant, Guillaume
Brillet, Benjamin
Briseño-Roa, Luis
Cadene, Martine
Augé-Gouillou, Corinne
author_sort Bouchet, Nicolas
collection PubMed
description 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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spelling pubmed-39028982014-01-27 cAMP protein kinase phosphorylates the Mos1 transposase and regulates its activity: evidences from mass spectrometry and biochemical analyses Bouchet, Nicolas Jaillet, Jérôme Gabant, Guillaume Brillet, Benjamin Briseño-Roa, Luis Cadene, Martine Augé-Gouillou, Corinne Nucleic Acids Res Nucleic Acid Enzymes 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. Oxford University Press 2014-01 2013-09-28 /pmc/articles/PMC3902898/ /pubmed/24081583 http://dx.doi.org/10.1093/nar/gkt874 Text en © The Author(s) 2013. Published by Oxford University Press. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Nucleic Acid Enzymes
Bouchet, Nicolas
Jaillet, Jérôme
Gabant, Guillaume
Brillet, Benjamin
Briseño-Roa, Luis
Cadene, Martine
Augé-Gouillou, Corinne
cAMP protein kinase phosphorylates the Mos1 transposase and regulates its activity: evidences from mass spectrometry and biochemical analyses
title cAMP protein kinase phosphorylates the Mos1 transposase and regulates its activity: evidences from mass spectrometry and biochemical analyses
title_full cAMP protein kinase phosphorylates the Mos1 transposase and regulates its activity: evidences from mass spectrometry and biochemical analyses
title_fullStr cAMP protein kinase phosphorylates the Mos1 transposase and regulates its activity: evidences from mass spectrometry and biochemical analyses
title_full_unstemmed cAMP protein kinase phosphorylates the Mos1 transposase and regulates its activity: evidences from mass spectrometry and biochemical analyses
title_short cAMP protein kinase phosphorylates the Mos1 transposase and regulates its activity: evidences from mass spectrometry and biochemical analyses
title_sort camp protein kinase phosphorylates the mos1 transposase and regulates its activity: evidences from mass spectrometry and biochemical analyses
topic Nucleic Acid Enzymes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3902898/
https://www.ncbi.nlm.nih.gov/pubmed/24081583
http://dx.doi.org/10.1093/nar/gkt874
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