Record Details

Chickpea transcription factor CaTLP1 interacts with protein kinases, modulates ROS accumulation and promotes ABA-mediated stomatal closure

NIPGR Digital Knowledge Repository (NDKR)

View Archive Info
 
 
Field Value
 
Title Chickpea transcription factor CaTLP1 interacts with protein kinases, modulates ROS accumulation and promotes ABA-mediated stomatal closure
 
Creator Wardhan, Vijay
Pandey, Aarti
Chakraborty, Subhra
Chakraborty, Niranjan
 
Subject Plant molecular biology
Plant physiology
Chickpea
transcription factor
protein kinases
 
Description Accepted date: 07 November 2016
Tubby and Tubby-like proteins (TLPs), in mammals, play critical roles in neural development, while its function in plants is largely unknown. We previously demonstrated that the chickpea TLP, CaTLP1, participates in osmotic stress response and might be associated with ABA-dependent network. However, how CaTLP1 is connected to ABA signaling remains unclear. The CaTLP1 was found to be engaged in ABA-mediated gene expression and stomatal closure. Complementation of the yeast yap1 mutant with CaTLP1 revealed its role in ROS scavenging. Furthermore, complementation of Arabidopsis attlp2 mutant displayed enhanced stress tolerance, indicating the functional conservation of TLPs across the species. The presence of ABA-responsive element along with other motifs in the proximal promoter regions of TLPs firmly established their involvement in stress signalling pathways. The CaTLP1 promoter driven GUS expression was restricted to the vegetative organs, especially stem and rosette leaves. Global protein expression profiling of wild-type, attlp2 and complemented Arabidopsis plants revealed 95 differentially expressed proteins, presumably involved in maintaining physiological and biological processes under dehydration. Immunoprecipitation assay revealed that protein kinases are most likely to interact with CaTLP1. This study provides the first demonstration that the TLPs act as module for ABA-mediated stomatal closure possibly via interaction with protein kinase.
This work was supported by grants (BT/PR13045/PBD/16/863/2009) from the Department of Biotechnology (DBT), Government of India to N.C. The authors thank Council of Scientific and Industrial Research (CSIR), Government of India for providing pre-doctoral fellowship to V.W. and the National Institute of Plant Genome Research, New Delhi for providing post-doctoral fellowship to A.P. We kindly acknowledge Dr. T. Nakagawa, Shimane University, Japan for the generous gift of destination vectors pGWB411, 433 and 441. We express our gratitude to Dr. David Bouchez, Institut Jean-Pierre Bourgin, Versailles, France for complete set of four pBiFP vectors.
 
Date 2017-05-03T06:14:35Z
2017-05-03T06:14:35Z
2016
 
Type Article
 
Identifier Scientific Reports, 6: 38121
2045-2322
http://59.163.192.83:8080/jspui/handle/123456789/740
https://www.nature.com/articles/srep38121
10.1038/srep38121
 
Language en_US
 
Publisher Nature Publishing Group