An enhancer mutant of Arabidopsis salt overly sensitive 3 mediates both ion homeostasis and the oxidative stress response
Document Type
Article
Publication Date
2007
Abstract
The myristoylated calcium sensor SOS3 and its interacting protein kinase, SOS2, play critical regulatory roles in salt tolerance. Mutations in either of these proteins render Arabidopsis thaliana plants hypersensitive to salt stress. We report here the isolation and characterization of a mutant called enh1-1 that enhances the salt sensitivity of sos3-1 and also causes increased salt sensitivity by itself. ENH1 encodes a chloroplast-localized protein with a PDZ domain at the N-terminal region and a rubredoxin domain in the C-terminal part. Rubredoxins are known to be involved in the reduction of superoxide in some anaerobic bacteria. The enh1-1 mutation causes enhanced accumulation of reactive oxygen species (ROS), particularly under salt stress. ROS also accumulate to higher levels in sos2-1 but not in sos3-1 mutants. The enh1-1 mutation does not enhance sos2-1 phenotypes. Also, enh1-1 and sos2-1 mutants, but not sos3-1 mutants, show increased sensitivity to oxidative stress. These results indicate that ENH1 functions in the detoxification of reactive oxygen species resulting from salt stress by participating in a new salt tolerance pathway that may involve SOS2 but not SOS3. Copyright © 2007, American Society for Microbiology. All Rights Reserved.
Publication Title
Molecular and cellular biology
Volume
27
First Page
5214
Last Page
5224
Recommended Citation
Zhu, J.; Fu, X.; Koo, Y.; Zhu, J.; Jenney, Francis E. Jr; Adams, Michael W.; Zhu, Y.; Shi, H.; Yub, S.; and al., et, "An enhancer mutant of Arabidopsis salt overly sensitive 3 mediates both ion homeostasis and the oxidative stress response" (2007). PCOM Scholarly Works. 619.
https://digitalcommons.pcom.edu/scholarly_papers/619
Comments
This article was published in Molecular and cellular biology, Volume 27, Issue 14, Pages 5214-5224.
The published version is available at http://dx.doi.org/10.1128/MCB.01989-06.Copyright © 2007 ASM.