Protein ID (intrinsic disorder) plays a significant, yet relatively unexplored role in transcription factors (TFs). In the present paper, analysis of the transcription regulatory domains (TRDs) of six phylogenetically representative, plant-specific NAC [no apical meristem, ATAF (Arabidopsis transcription activation factor), cup-shaped cotyledon] TFs shows that the domains are present in similar average pre-molten or molten globule-like states, but have different patterns of order/disorder and MoRFs (molecular recognition features). ANAC046 (Arabidopsis NAC 046) was selected for further studies because of its simple MoRF pattern and its ability to interact with RCD1 (radical-induced cell death 1). Experiments in yeast and thermodynamic characterization suggest that its single MoRF region is sufficient for both transcriptional activation and interaction with RCD1. The remainder of the large regulatory domain is unlikely to contribute to the interaction, since the domain and truncations thereof have similar affinities for RCD1, which are also similar for ANAC013–RCD1 interactions. However, different enthalpic and entropic contributions to binding were revealed for ANAC046 and ANAC013, suggestive of differences in binding mechanisms. Although substitution of both hydrophobic and acidic residues of the ANAC046 MoRF region abolished binding, substitution of other residues, even with α-helix-breaking proline, was less disruptive. Together, the biophysical analyses suggest that RCD1–ANAC046 complex formation does not involve folding-upon-binding, but rather fuzziness or an unknown structure in ANAC046. We suggest that the ANAC046 regulatory domain functions as an entropic chain with a terminal hot spot interacting with RCD1. RCD1, a cellular hub, may be able to interact with many different TFs by exploiting their ID-based flexibility, as demonstrated for its interactions with ANAC046 and ANAC013.
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January 2015
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Research Article|
January 06 2015
Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1
Charlotte O’Shea;
Charlotte O’Shea
*Department of Biology, University of Copenhagen, 5 Ole Maaloesvej, Copenhagen DK-2200, Denmark
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Mikael Kryger;
Mikael Kryger
*Department of Biology, University of Copenhagen, 5 Ole Maaloesvej, Copenhagen DK-2200, Denmark
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Emil G. P. Stender;
Emil G. P. Stender
*Department of Biology, University of Copenhagen, 5 Ole Maaloesvej, Copenhagen DK-2200, Denmark
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Birthe B. Kragelund;
Birthe B. Kragelund
*Department of Biology, University of Copenhagen, 5 Ole Maaloesvej, Copenhagen DK-2200, Denmark
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Martin Willemoës;
Martin Willemoës
*Department of Biology, University of Copenhagen, 5 Ole Maaloesvej, Copenhagen DK-2200, Denmark
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Karen Skriver
Karen Skriver
1
*Department of Biology, University of Copenhagen, 5 Ole Maaloesvej, Copenhagen DK-2200, Denmark
1To whom correspondence should be addressed (email kskriver@bio.ku.dk).
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Publisher: Portland Press Ltd
Received:
August 12 2014
Revision Received:
October 24 2014
Accepted:
October 28 2014
Accepted Manuscript online:
October 28 2014
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2015 Biochemical Society
2015
Biochem J (2015) 465 (2): 281–294.
Article history
Received:
August 12 2014
Revision Received:
October 24 2014
Accepted:
October 28 2014
Accepted Manuscript online:
October 28 2014
Citation
Charlotte O’Shea, Mikael Kryger, Emil G. P. Stender, Birthe B. Kragelund, Martin Willemoës, Karen Skriver; Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. Biochem J 15 January 2015; 465 (2): 281–294. doi: https://doi.org/10.1042/BJ20141045
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