Calmodulin-binding protein CBP60g is a positive regulator of both disease resistance and drought tolerance in Arabidopsis
Plant Cell Reports, ISSN: 0721-7714, Vol: 31, Issue: 7, Page: 1269-1281
2012
- 94Citations
- 2Usage
- 108Captures
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Metrics Details
- Citations94
- Citation Indexes94
- 94
- CrossRef36
- Usage2
- Abstract Views2
- Captures108
- Readers108
- 108
Article Description
Calmodulin-binding proteins (CBPs) have been known to be involved in both biotic and abiotic stress responses. Recently, two closely related CBPs, Arabidopsis SAR Deficient 1 and CBP60g, were found to belong to a new family of transcription factors that regulate salicylic acid (SA) biosynthesis triggered by microbe-associated molecular patterns. In this study, we found that overexpression of CBP60g in Arabidopsis caused elevated SA accumulation, increased expression of the defense genes, and enhanced resistance to Pseudomonas syringae. In addition to the enhanced defense response, the CBP60g overexpression lines showed hypersensitivity to abscisic acid (ABA) and enhanced tolerance to drought stress. We also found that treatment with ABA and drought stress leads to a higher expression level of the ICS1 gene, which encodes isochorismate synthase, in the CBP60g overexpression lines than in the wild-type control plants. Our results suggest that CBP60g serves as a molecular link that positively regulates ABA-and SA-mediated pathways in plants. Key message Overexpression of CBP60g in Arabidopsis enhanced the defense response, hypersensitivity to abscisic acid and tolerance to drought stress. © 2012 Springer-Verlag.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84862492158&origin=inward; http://dx.doi.org/10.1007/s00299-012-1247-7; http://www.ncbi.nlm.nih.gov/pubmed/22466450; http://link.springer.com/10.1007/s00299-012-1247-7; https://repository.hkbu.edu.hk/hkbu_staff_publication/1280; https://repository.hkbu.edu.hk/cgi/viewcontent.cgi?article=2294&context=hkbu_staff_publication; https://dx.doi.org/10.1007/s00299-012-1247-7; https://link.springer.com/article/10.1007/s00299-012-1247-7; http://www.springerlink.com/index/10.1007/s00299-012-1247-7; http://www.springerlink.com/index/pdf/10.1007/s00299-012-1247-7
Springer Science and Business Media LLC
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