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. 2013 Apr 11:4:98.
doi: 10.3389/fpls.2013.00098. eCollection 2013.

Regulate and be regulated: integration of defense and other signals by the AtMYB30 transcription factor

Sylvain Raffaele  1 , Susana Rivas
Affiliations

Regulate and be regulated: integration of defense and other signals by the AtMYB30 transcription factor

Sylvain Raffaele et al. Front Plant Sci. .

Abstract

Transcriptional regulation in host cells plays a crucial role in the establishment of plant defense and associated cell death in response to pathogen attack. Here, we review our current knowledge of the transcriptional control of plant defenses with a focus on the MYB family of transcription factors (TFs). Within this family, the Arabidopsis MYB protein AtMYB30 is a key regulator of plant defenses and one of the best characterized MYB regulators directing defense-related transcriptional responses. The crucial role played by AtMYB30 in the regulation of plant disease resistance is underlined by the finding that AtMYB30 is targeted by the Xanthomonas type III effector XopD resulting in suppression of AtMYB30-mediated plant defenses. Moreover, the function of AtMYB30 is also tightly controlled by plant cells through protein-protein interactions and post-translational modifications (PTMs). AtMYB30 studies highlight the importance of cellular dynamics for defense-associated gene regulation in plants. Finally, we discuss how AtMYB30 and other MYB TFs mediate the interplay between disease resistance and other stress responses.

Keywords: Arabidopsis; AtMYB30; MYB transcription factor; hypersensitive response; plant defense; stress responses; transcriptional regulation.

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Figures

Figure 1
Figure 1
Simplified model for the simultaneous regulation of AtMYB30-mediated HR cell death through interaction with AtsPLA2−α and MIEL1. The action of with AtsPLA2−α and MIEL1 on AtMYB30-mediated HR development is presented in cells challenged with bacterial inoculation (A) and peripheral cells (B). Activity of the bacterial XopD effector is shown in red. See the text for details.
Figure 2
Figure 2
AtMYB30 sequence analysis: relationship with other MYBs, protein motifs and predicted structure. (A) Relationship between MYB TFs of the subgroup S1 (from Dubos et al., 2010). (B) Predicted structure of AtMYB30 DNA binding domain bound to DNA (gray). The model was predicted using the I-TASSER server and rendered with UCSF Chimera. (C) Sequence analysis of AtMYB30 protein. The conservation between members of subgroup S1 was inferred from a MUSCLE alignment and colored using JALVIEW. Alpha helices and DNA binding sites were predicted using the I-TASSER server. MYB domains were identified using INTERPROSCAN. Phosphorylation, sumoylation and ubiquitation sites were predicted using PhosphAt, Sumoplot and Ubpred respectively.
See this image and copyright information in PMC

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