Abstract
Many plant genes have their expression modulated by stress conditions. Here, we used Arabidopsis FtsH5 protease, which expression is regulated by light stress, as bait in a yeast two-hybrid screen to search for new proteins involved in the stress response. As a result, we found FIP (FtsH5 Interacting Protein), which possesses an amino proximal cleavable transit peptide, a hydrophobic membrane-anchoring region, and a carboxyl proximal C4-type zinc-finger domain. In vivo experiments using FIP fused to green fluorescent protein (GFP) showed a plastid localization. This finding was corroborated by chloroplast import assays that showed FIP inserted in the thylakoid membrane. FIP expression was down-regulated in plants exposed to high light intensity, oxidative, salt, and osmotic stresses, whereas mutant plants expressing low levels of FIP were more tolerant to these abiotic stresses. Our data shows a new thylakoid-membrane protein involved with abiotic stress response in Arabidopsis thaliana.
Highlights
Plants are constantly exposed to biotic and abiotic environmental stress conditions
FtsH protein was first described in Escherichia coli, where it is involved in the proteolysis of membrane proteins (Ito and Akiyama, 2005; Wagner et al, 2012) and, most importantly, the degradation of heat shock sigma factor σ32
The yeast two-hybrid system was employed to identify proteins involved in the stress response mechanism that potentially interacts with FtsH protein in chloroplasts, since FtsH is directly involved in stress response in plants
Summary
Plants are constantly exposed to biotic and abiotic environmental stress conditions. These parameters include water and nutrients availability, microorganism population in soil, predators, pests, salinity, temperature variance, light incidence, etc. FtsH proteases belong to the AAA+ (ATPase Associated with diverse cellular Activities) family (Tomoyasu et al, 1993; Ogura and Wilkinson, 2001; Kato and Sakamoto, 2010; Liu et al, 2010; Nixon et al, 2010) and their functions in cells are known to some extent (Ogura et al, 1999; Adam et al, 2006). FtsH protein was first described in Escherichia coli, where it is involved in the proteolysis of membrane proteins (Ito and Akiyama, 2005; Wagner et al, 2012) and, most importantly, the degradation of heat shock sigma factor σ32
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