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Researchers Decipher How ROS Sensor Acts in Chloroplast

Jul 06, 2016

A potential singlet oxygen (1O2) sensing complex constituted by EXECUTER1 (EX1) protein and ATP-dependent FtsH metalloprotease was found to be assembled in thylakoid membrane and appears to be an integral component of 1O2-triggered chloroplast-to-nucleus retrograde signaling under photo-oxidative stress condition.
Research groups led by Prof. Klaus Apel from Boyce Thompson Institute at Cornell University in New York, Ithaca and by Prof. Chanhong Kim at Shanghai Center for Plant Stress Biology (PSC), Shanghai Institutes for Biological Sciences of Chinese Academy of Sciences have recently addressed a question about how chloroplast-generated 1O2, one of the reactive oxygen species (ROS), activates distinct retrograde signaling cascades via: volatile signaling molecules and EX1, a nuclear-encoded and plastid-targeted protein. The intriguing results of this study were published in the recent issue of Proc Natl Acad Sci.

Uncovering ROS sensor has long been an inquisitive prospective and the most changeable subject matter for stress biologists since cells generate ROS almost simultaneously in various subcellular compartments in response to multitude of environmental factors. Amongst, chloroplast has been widely accepted as one of the major subcellular organelles generating chemically distinct ROS including singlet oxygen, hydrogen peroxide and superoxide anion in light-dependent manner.

Mounting evidence suggests that chloroplast acts as environmental sensor as the rapid ROS accumulation and the concurrent redox changes alter nuclear gene expression changes despite the fact that chloroplast and nucleus are physical distinct. Interestingly, a potential 1O2 sensor protein EX1 residing in chloroplast was shown to mediate retrograde signaling induced by chloroplast-generated 1O2 in Arabidopsis flu mutant.

Recently, β-carotene integrated in photosystem II (PSII) reaction center at the ‘grana core’ was found to be a potential 1O2 sensor. It has also been proved that its volatile derivative β-cyclocitral induces similar nuclear gene expression changes as those in flu, priming acclimation and stress responses. β-cyclocitral mediated signaling was shown to be independent of EX1 and thus the question regarding the biological relevance of these two distinct signaling has been questioned.

WANG et al. showed that EX1 proteins mostly reside in the ‘grana margin’ where PSII repair takes place and relays 1O2 signaling from there itself, and perhaps that’s how EX1 proteins constitutes a distinct signaling as compared to β-carotene present in the grana core. Moreover, EX1 proteins decline rapidly upon 1O2 burst by FtsH metalloprotease which functions in photosystem II repair in grana margin. Indeed, the inactivation of FtsH in flu mutant significantly compromises the stress responses, suggesting that the proteolytic degradation of EX1 seems to be an integral part of the initiation of 1O2 signaling.

"Finding 1O2 sensor and understanding its mode of action in Arabidopsis open a new paradigm of plant stress biology to decipher plant-environment interaction since even minor fluctuations of light and temperature lead to accumulation of ROS in chloroplast. Once we elucidate the underlying molecular mechanism of 1O2 sensor, next we will try to find a genuine signaling molecule, which seems to be released upon its degradation and concurrently induces retrograde signaling, priming acclimation and programmed cell death.” says Professor Chanhong Kim.

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