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Title: The tomato DWD motif-containing protein DDI1 interacts with the CUL4–DDB1-based ubiquitin ligase and plays a pivotal role in abiotic stress responses

Abstract

Highlights: • We identify DDI1 as a DAMAGED DNA BINDING PROTEIN1 (DDB1)-interacting protein. • DDI1 interacts with the CUL4–DDB1-based ubiquitin ligase in the nucleus. • DDI1 plays a positive role in regulating abiotic stress response in tomato. - Abstract: CULLIN4(CUL4)–DAMAGED DNA BINDING PROTEIN1 (DDB1)-based ubiquitin ligase plays significant roles in multiple physiological processes via ubiquitination-mediated degradation of relevant target proteins. The DDB1–CUL4-associated factor (DCAF) acts as substrate receptor in the CUL4–DDB1 ubiquitin ligase complex and determines substrate specificity. In this study, we identified a tomato (Solanum lycopersicum) DDB1-interacting (DDI1) protein as a DCAF protein involved in response to abiotic stresses, including UV radiation, high salinity and osmotic stress. Co-immunoprecipitation and bimolecular fluorescence complementation assay indicated that DDI1 associates with CUL4–DDB1 in the nucleus. Quantitative RT-PCR analysis indicated the DDI1 gene is induced by salt, mannitol and UV-C treatment. Moreover, transgenic tomato plants with overexpression or knockdown of the DDI1 gene exhibited enhanced or attenuated tolerance to salt/mannitol/UV-C, respectively. Thus, our data suggest that DDI1 functions as a substrate receptor of the CUL4–DDB1 ubiquitin ligase, positively regulating abiotic stress response in tomato.

Authors:
 [1];  [2];  [1];  [1];  [2];  [3];  [1]
  1. Ministry of Education Key Laboratory for Bio-resource and Eco-environment, College of Life Science, State Key Laboratory of Hydraulics and Mountain River Engineering, Sichuan University, Chengdu 610064 (China)
  2. School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009 (China)
  3. Department of Plant, Soil and Entomological Sciences, University of Idaho, Moscow, ID 83844-2339 (United States)
Publication Date:
OSTI Identifier:
22416691
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 450; Journal Issue: 4; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; FLUORESCENCE; GENES; LIGASES; POLYMERASE CHAIN REACTION; RECEPTORS; SALINITY; SOLANUM; SPECIFICITY; SUBSTRATES; TOLERANCE; TOMATOES; ULTRAVIOLET RADIATION

Citation Formats

Miao, Min, School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009, Department of Plant, Soil and Entomological Sciences, University of Idaho, Moscow, ID 83844-2339, Zhu, Yunye, Qiao, Maiju, Tang, Xiaofeng, School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009, Zhao, Wei, Xiao, Fangming, Liu, Yongsheng, and School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009. The tomato DWD motif-containing protein DDI1 interacts with the CUL4–DDB1-based ubiquitin ligase and plays a pivotal role in abiotic stress responses. United States: N. p., 2014. Web. doi:10.1016/J.BBRC.2014.07.011.
Miao, Min, School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009, Department of Plant, Soil and Entomological Sciences, University of Idaho, Moscow, ID 83844-2339, Zhu, Yunye, Qiao, Maiju, Tang, Xiaofeng, School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009, Zhao, Wei, Xiao, Fangming, Liu, Yongsheng, & School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009. The tomato DWD motif-containing protein DDI1 interacts with the CUL4–DDB1-based ubiquitin ligase and plays a pivotal role in abiotic stress responses. United States. https://doi.org/10.1016/J.BBRC.2014.07.011
Miao, Min, School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009, Department of Plant, Soil and Entomological Sciences, University of Idaho, Moscow, ID 83844-2339, Zhu, Yunye, Qiao, Maiju, Tang, Xiaofeng, School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009, Zhao, Wei, Xiao, Fangming, Liu, Yongsheng, and School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009. 2014. "The tomato DWD motif-containing protein DDI1 interacts with the CUL4–DDB1-based ubiquitin ligase and plays a pivotal role in abiotic stress responses". United States. https://doi.org/10.1016/J.BBRC.2014.07.011.
@article{osti_22416691,
title = {The tomato DWD motif-containing protein DDI1 interacts with the CUL4–DDB1-based ubiquitin ligase and plays a pivotal role in abiotic stress responses},
author = {Miao, Min and School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009 and Department of Plant, Soil and Entomological Sciences, University of Idaho, Moscow, ID 83844-2339 and Zhu, Yunye and Qiao, Maiju and Tang, Xiaofeng and School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009 and Zhao, Wei and Xiao, Fangming and Liu, Yongsheng and School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009},
abstractNote = {Highlights: • We identify DDI1 as a DAMAGED DNA BINDING PROTEIN1 (DDB1)-interacting protein. • DDI1 interacts with the CUL4–DDB1-based ubiquitin ligase in the nucleus. • DDI1 plays a positive role in regulating abiotic stress response in tomato. - Abstract: CULLIN4(CUL4)–DAMAGED DNA BINDING PROTEIN1 (DDB1)-based ubiquitin ligase plays significant roles in multiple physiological processes via ubiquitination-mediated degradation of relevant target proteins. The DDB1–CUL4-associated factor (DCAF) acts as substrate receptor in the CUL4–DDB1 ubiquitin ligase complex and determines substrate specificity. In this study, we identified a tomato (Solanum lycopersicum) DDB1-interacting (DDI1) protein as a DCAF protein involved in response to abiotic stresses, including UV radiation, high salinity and osmotic stress. Co-immunoprecipitation and bimolecular fluorescence complementation assay indicated that DDI1 associates with CUL4–DDB1 in the nucleus. Quantitative RT-PCR analysis indicated the DDI1 gene is induced by salt, mannitol and UV-C treatment. Moreover, transgenic tomato plants with overexpression or knockdown of the DDI1 gene exhibited enhanced or attenuated tolerance to salt/mannitol/UV-C, respectively. Thus, our data suggest that DDI1 functions as a substrate receptor of the CUL4–DDB1 ubiquitin ligase, positively regulating abiotic stress response in tomato.},
doi = {10.1016/J.BBRC.2014.07.011},
url = {https://www.osti.gov/biblio/22416691}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 4,
volume = 450,
place = {United States},
year = {Fri Aug 08 00:00:00 EDT 2014},
month = {Fri Aug 08 00:00:00 EDT 2014}
}