MODD Mediates Deactivation and Degradation of OsbZIP46 to Negatively Regulate ABA Signaling and Drought Resistance in Rice. Issue 9 (28th July 2016)
- Record Type:
- Journal Article
- Title:
- MODD Mediates Deactivation and Degradation of OsbZIP46 to Negatively Regulate ABA Signaling and Drought Resistance in Rice. Issue 9 (28th July 2016)
- Main Title:
- MODD Mediates Deactivation and Degradation of OsbZIP46 to Negatively Regulate ABA Signaling and Drought Resistance in Rice
- Authors:
- Tang, Ning
Ma, Siqi
Zong, Wei
Yang, Ning
Lv, Yan
Yan, Chun
Guo, Zilong
Li, Jie
Li, Xu
Xiang, Yong
Song, Huazhi
Xiao, Jinghua
Li, Xianghua
Xiong, Lizhong - Abstract:
- Abstract : MODD negatively regulates OsbZIP46 activity and stability through HDAC-related chromatin remodeling and PUB70-mediated ubiquitination, respectively, to fine-tune ABA signaling and drought resistance. Abstract: Plants have evolved complicated protective mechanisms to survive adverse conditions. Previously, we reported that the transcription factor OsbZIP46 regulates abscisic acid (ABA ) signaling-mediated drought tolerance in rice ( Oryza sativa ) by modulating stress-related genes. An intrinsic D domain represses OsbZIP46 activity, but the detailed mechanism for the repression of OsbZIP46 activation remains unknown. Here, we report an OsbZIP46-interacting protein, MODD (Mediator of OsbZIP46 deactivation and degradation), which is homologous to the Arabidopsis thaliana ABSCISIC ACID-INSENSITIVE5 binding protein AFP. MODD was induced by ABA and drought stress, but the induction was much slower than that of OsbZIP46 . In contrast to OsbZIP46, MODD negatively regulates ABA signaling and drought tolerance, and inhibits the expression of OsbZIP46 target genes. We found that MODD negatively regulates OsbZIP46 activity and stability. MODD represses OsbZIP46 activity via interaction with the OsTPR3-HDA702 corepressor complex and downregulation of the histone acetylation level at OsbZIP46 target genes. MODD promotes OsbZIP46 degradation via interaction with the U-box type ubiquitin E3 ligase OsPUB70. Interestingly, the D domain is required for both deactivation andAbstract : MODD negatively regulates OsbZIP46 activity and stability through HDAC-related chromatin remodeling and PUB70-mediated ubiquitination, respectively, to fine-tune ABA signaling and drought resistance. Abstract: Plants have evolved complicated protective mechanisms to survive adverse conditions. Previously, we reported that the transcription factor OsbZIP46 regulates abscisic acid (ABA ) signaling-mediated drought tolerance in rice ( Oryza sativa ) by modulating stress-related genes. An intrinsic D domain represses OsbZIP46 activity, but the detailed mechanism for the repression of OsbZIP46 activation remains unknown. Here, we report an OsbZIP46-interacting protein, MODD (Mediator of OsbZIP46 deactivation and degradation), which is homologous to the Arabidopsis thaliana ABSCISIC ACID-INSENSITIVE5 binding protein AFP. MODD was induced by ABA and drought stress, but the induction was much slower than that of OsbZIP46 . In contrast to OsbZIP46, MODD negatively regulates ABA signaling and drought tolerance, and inhibits the expression of OsbZIP46 target genes. We found that MODD negatively regulates OsbZIP46 activity and stability. MODD represses OsbZIP46 activity via interaction with the OsTPR3-HDA702 corepressor complex and downregulation of the histone acetylation level at OsbZIP46 target genes. MODD promotes OsbZIP46 degradation via interaction with the U-box type ubiquitin E3 ligase OsPUB70. Interestingly, the D domain is required for both deactivation and degradation of OsbZIP46 via its interaction with MODD. These findings show that plants fine-tune their drought responses by elaborate regulatory mechanisms, including the coordination of activity and stability of key transcription factors. … (more)
- Is Part Of:
- The Plant Cell. Volume 28:Issue 9(2016)
- Journal:
- The Plant Cell
- Issue:
- Volume 28:Issue 9(2016)
- Issue Display:
- Volume 28, Issue 9 (2016)
- Year:
- 2016
- Volume:
- 28
- Issue:
- 9
- Issue Sort Value:
- 2016-0028-0009-0000
- Page Start:
- 2161
- Page End:
- 2177
- Publication Date:
- 2016-07-28
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.16.00171 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16319.xml