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A Membrane-Bound NAC Transcription Factor, ANAC017, Mediates Mitochondrial Retrograde Signaling in Arabidopsis
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2013 (English)In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 25, no 9, 3450-3471 p.Article in journal (Refereed) Published
Abstract [en]

Plants require daily coordinated regulation of energy metabolism for optimal growth and survival and therefore need to integrate cellular responses with both mitochondrial and plastid retrograde signaling. Using a forward genetic screen to characterize regulators of alternative oxidase1a (rao) mutants, we identified RAO2/Arabidopsis NAC domain-containing protein17 (ANAC017) as a direct positive regulator of AOX1a. RAO2/ANAC017 is targeted to connections and junctions in the endoplasmic reticulum (ER) and F-actin via a C-terminal transmembrane (TM) domain. A consensus rhomboid protease cleavage site is present in ANAC017 just prior to the predicted TM domain. Furthermore, addition of the rhomboid protease inhibitor N-p-Tosyl-L-Phe chloromethyl abolishes the induction of AOX1a upon antimycin A treatment. Simultaneous fluorescent tagging of ANAC017 with N-terminal red fluorescent protein (RFP) and C-terminal green fluorescent protein (GFP) revealed that the N-terminal RFP domain migrated into the nucleus, while the C-terminal GFP tag remained in the ER. Genome-wide analysis of the transcriptional network regulated by RAO2/ANAC017 under stress treatment revealed that RAO2/ANAC017 function was necessary for > 85% of the changes observed as a primary response to cytosolic hydrogen peroxide (H2O2), but only; 33% of transcriptional changes observed in response to antimycin A treatment. Plants with mutated rao2/anac017 were more stress sensitive, whereas a gain-of-function mutation resulted in plants that had lower cellular levels of H2O2 under untreated conditions.

Place, publisher, year, edition, pages
2013. Vol. 25, no 9, 3450-3471 p.
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:su:diva-96667DOI: 10.1105/tpc.113.113985ISI: 000326287100024OAI: diva2:667399


Available from: 2013-11-26 Created: 2013-11-25 Last updated: 2013-11-26Bibliographically approved

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Kmiec, Beata
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Department of Biochemistry and Biophysics
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