Arabidopsis proteins with a transposon-related domain act in gene silencing
Yoko Ikeda,
Thierry Pélissier,
Pierre Bourguet,
Claude Becker,
Marie-Noëlle Pouch-Pélissier,
Romain Pogorelcnik,
Magdalena Weingartner,
Detlef Weigel,
Jean-Marc Deragon and
Olivier Mathieu ()
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Yoko Ikeda: Université Clermont Auvergne, CNRS, Inserm, GReD
Thierry Pélissier: Université Clermont Auvergne, CNRS, Inserm, GReD
Pierre Bourguet: Université Clermont Auvergne, CNRS, Inserm, GReD
Claude Becker: Max Planck Institute for Developmental Biology
Marie-Noëlle Pouch-Pélissier: Université Clermont Auvergne, CNRS, Inserm, GReD
Romain Pogorelcnik: Université Clermont Auvergne, CNRS, Inserm, GReD
Magdalena Weingartner: Molekulare Pflanzenphysiologie, Biozentrum Klein Flottbek, Universität Hamburg
Detlef Weigel: Max Planck Institute for Developmental Biology
Jean-Marc Deragon: Laboratoire Génome et Développement des Plantes (LGDP), CNRS, UMR5096, Université de Perpignan Via Domitia
Olivier Mathieu: Université Clermont Auvergne, CNRS, Inserm, GReD
Nature Communications, 2017, vol. 8, issue 1, 1-10
Abstract:
Abstract Transposable elements (TEs) are prevalent in most eukaryotes, and host genomes have devised silencing strategies to rein in TE activity. One of these, transcriptional silencing, is generally associated with DNA methylation and short interfering RNAs. Here we show that the Arabidopsis genes MAIL1 and MAIN define an alternative silencing pathway independent of DNA methylation and short interfering RNAs. Mutants for MAIL1 or MAIN exhibit release of silencing and appear to show impaired condensation of pericentromeric heterochromatin. Phylogenetic analysis suggests not only that MAIL1 and MAIN encode a retrotransposon-related plant mobile domain, but also that host plant mobile domains were captured by DNA transposons during plant evolution. Our results reveal a role for Arabidopsis proteins with a transposon-related domain in gene silencing.
Date: 2017
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15122
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DOI: 10.1038/ncomms15122
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