• Bulletin of the Korean Chemical Society
• /
• v.32 no.9
• /
• pp.3497-3500
• /
• 2011

• Animal cells and systems
• /
• v.9 no.3
• /
• pp.139-144
• /
• 2005

The attractant (orange light) or repellent (white light) signal is transmitted from SRI (Sensory Rhodopsin I) via protein-protein interaction with its transducer Htrl (Halobacterial Transducer for Sensory Rhodopsin I) which in turn controls a cytoplasmic phospho-transfer pathway that modulates flagella motor switching in Halobacterium salinarum. Some mutations in both SRI and Htrl showed an unusual mutant phenotype called inverted signaling, in which the cell produces a repellent response to normally attractant light. Twelve mutations at the Glutamate 56 (E56) position in the second transmembrane helix of Htrl were introduced by site-specific random mutagenesis. Almost all E56 mutants showed orange-light inverted responses in pH and temperature-dependent manners except E56D and E56Y. Except for these two mutants, all mutants accelerated the $S_{373}$ decay compared to wild-type at $18^{\circ}C$. This supported that there is an interaction between SRI and the second transmembrane of Htrl. Also a structural model of Htrl based on the Tar crystal structure and the secondary structure prediction program proposed the E56 residue to be in the middle of the proton channel. The most important observation is that the E56 mutant provides the evidence that this residue is very sensitive for signal relay, which can be explained by the open and closed conformations of the channel (A and R conformations) in SRI, as was postulated by the unified conformational shuttling model for transport and signaling.

• Interdisciplinary Bio Central
• /
• v.1 no.1
• /
• pp.1.1-1.5
• /
• 2009

Many organisms control their physiology and behavior in response to the local light environment, which is first perceived by photoreceptors that undergo light-dependent conformational changes. Phytochromes are one of the major photoreceptors in plants, controlling wide aspects of plant physiology by recognizing the light in red (R) and far-red (FR) spectra. Higher plants have two types of phytochromes; the photo-labile type I (phyA in Arabidopsis) and photo-stable type II (phyB-E in Arabidopsis). Phytochrome B (phyB), a member of the type II phytochromes in Arabidopsis, shows classical R and FR reversibility between the inter-convertible photoisomers, Pr and Pfr. Interestingly, the Pr and Pfr isomers show partitioning in the cytosol and nucleus, respectively. In the over 50 years since its discovery, it has been thought that the type II phytochromes only function to mediate R light. As described in the text, we have now discovered phyB has an active function in FR light. Even striking is that the R and FR light exert an opposite effect. Thus, FR light is not simply nullifying the R effect but has an opposing effect to R light. What is more interesting is that the phyB-mediated actions of FR and R light occur at different cellular compartment of the plant cell, cytosol and nucleus, respectively, which was proven through utilization of the cytosolic and nuclear-localized mutant versions of phyB. Our observations thus shoot down a major dogma in plant physiology and will be considered highly provocative in phytochrome function. We argue that it would make much more sense that plants utilize the two isoforms rather than only one form, to effectively monitor the changing environmental light information and to incorporate the information into their developmental programs.

• Journal of Plant Biotechnology
• /
• v.33 no.1
• /
• pp.1-9
• /
• 2006

Peroxiredoxins (Prxs) are ubiquitously distributed and play important functions in diverse cellular signaling systems. The proteins are largely classified into three groups, such as typical 2-Cys Prx, atypical 2-Cys Prx, and 1-Cys Prx, that are distinguished by their catalytic mechanisms and number of Cys residues. From the three classes of Prxs, the typical 2-Cys Prx containing the two-conserved Cys residues at its N-terminus and C-terminus catalyzes $H_2O_2$ with the use of thioredoxin (Trx) as an electron donor. During the catalytic cycle, the N-terminal Cys residue undergoes a peroxide-dependent oxidation to sulfenic acid, which can be further oxidized to sulfinic acid at the presence of high concentrations of $H_2O_2$ and a Trx system containing Trx, Trx reductase, and NADPH. The sulfinic acid form of 2-Cys Prx is reduced by the action of sulfiredoxin which requires ATP as an energy source. Under the strong oxidative or heat shock stress conditions, 2-Cys Prx in eukaryotes rapidly switches its protein structure from low-molecular-weight species to high-molecular-weight protein structures. In accordance with its structural changes, the protein concomitantly triggers functional switching from a peroxidase to a molecular chaperone, which can protect its substrate denaturation from external stress. In addition to its N-terminal active site, the C-terminal domain including 'YF-motif' of 2-Cys Prx plays a critical role in the structural changes. Therefore, the C-terminal truncated 2-Cys Prxs are not able to regulate their protein structures and highly resistant to $H_2O_2$-dependent hyperoxidation, suggesting that the reaction is guided by the peroxidatic Cys residue. Based on the results, it may be concluded that the peroxidatic Cys of 2-Cys Prx acts as an '$H_2O_2$-sensor' in the cells. The oxidative stress-dependent regulation of 2-Cys Prx provides a means of defense systems in cells to adapt stress conditions by activating intracellular defense signaling pathways. Particularly, 2-Cys Prxs in plants are localized in chloroplasts with a dynamic protein structure. The protein undergoes conformational changes again oxidative stress. Depending on a redox-potential of the chloroplasts, the plant 2-Cys Prx forms super-molecular weight protein structures, which attach to the thylakoid membranes in a reversible manner.