The Arabidopsis transcription factor bZIP11 activates auxin-mediated transcription by recruiting the histone acetylation machinery

Christoph Weiste and Wolfgang Dröge-Laser ()
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Christoph Weiste: Julius-von-Sachs-Institut, Pharmazeutische Biologie, Julius-Maximilians-Universität Würzburg, Julius-von-Sachs-Platz 2
Wolfgang Dröge-Laser: Julius-von-Sachs-Institut, Pharmazeutische Biologie, Julius-Maximilians-Universität Würzburg, Julius-von-Sachs-Platz 2

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: Abstract In higher plants, the hormone auxin orchestrates a diverse array of developmental and environmental responses mainly exerted via transcriptional control. In its absence, auxin-mediated transcription is postulated to be repressed by histone deacetylases, which convert chromatin into a highly packed inactive state. Here we present a converse mechanism where Arabidopsis bZIP11-related basic leucine zipper (bZIP) transcription factors interact via an amino-terminal activation domain with ADA2b adapter proteins to recruit the histone acetylation machinery to specific auxin-responsive genes. Gain, loss-of-function and pharmacological approaches as well as chromatin immunoprecipitation experiments addressing various components of the recruitment and acetylation machinery substantiate the proposed mechanism. Importantly, G-box-related cis-elements, frequently found in auxin-induced promoters, are shown to bind bZIP11-related bZIPs and to function as quantitative modulators of auxin-induced transcription. In conclusion, we describe a regulatory activation mechanism that serves as a rheostat to modulate auxin-mediated responses.

Date: 2014
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DOI: 10.1038/ncomms4883

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