• Journal of Plant Biology
• /
• v.35 no.3
• /
• pp.247-252
• /
• 1992

The effect of iso-butanol on the electron transport rate of PS I and PS II was investigated in isolated spinach chloroplasts. In photosystem I, the rate of electron transport increased in the presence of 1 to 4% of isobutanol but decreased in 5 to 9% of iso-butanol. But in photosystem II, the rate of electron transport decreased when treated with 0.2 to 1% of iso-butanol. The inhibitory effect of isomers of butanol on PS II electron transport rate increased in the order of 2-butanol, tert-butanol, iso-butanol and I-butanol. This means that PS II activity was affected according to the arrangement of carbon atoms in butanol. The inhibitory effect of iso-butanol reduced when DPC was added in the solution. This means that iso-butanol affects PS II reduction side of thylakoid membrane primarily. The inhibitory effect of iso-butanol was reduced when $Mn^{2+},\;C^{2+}$ or BSA were added in the solution. PS II activity was restored when 1% iso-butanol treated chloroplast solution was diluted to twentyfold or when $Mn^{2+},\;C^{2+}$ or BSA was added to the diluted solution. However, the SDS-PAGE banding pattern of thylakoid membrane proteins was similar even in 2% iso-butanol treated chloroplasts and the control ones. Only in 5% iso-butanol treated chloroplasts these bands were very weak. These observations suggest that low concentrations of iso-butanol releases manganese and calcium ions from chloroplasts and inhibits the electron transport system. This inhibitory effect can be reversible in low concenterations but in high concentrations the inhibitory effect of iso-butanol become irreversible.rsible.

• Journal of Life Science
• /
• v.27 no.1
• /
• pp.100-121
• /
• 2017

The sexual reproduction of the unicellular green alga Chlamydomonas is reviewed for a comprehensive understanding of the complex processes. The sexual life cycle of C. reinhardtii is distinguished into five main stages: gametogenesis, gamete activation, cell fusion, zygote maturation, and meiosis and germination. Gametogenesis is induced by nitrogen starvation in the environment. C. reinhardtii has two mating types: mating type plus ($mt^+$) and mating type minus ($mt^-$), controlled by a single complex mating type locus ($MT^+$ or $MT^-$) on linkage group VI. In the early gametogenesis agglutinins are synthesized. The $mt^+$ and $mt^-$ agglutinins are encoded by the autosomal genes SAG1 (Sexual AGglutination1) and SAD1 (Sexual ADhesion1), respectively. The agglutinins are responsible for the flagellar adhesion of the two mating type of gametes. The flagellar adhesion initiates a cAMP mediated signal transduction pathways and activates the flagellar tips. In response to the cAMP signal, mating structures between two flagella are activated. The $mt^+$ and $mt^-$ gamete-specific fusion proteins, Fus1 and Hap2/Gcs1, are present on the plasma membrane of the two mating structures. Contact of the two mating structures leads to develop a fertilization tubule forming a cytoplasmic bridge between the two gametes. Upon fusion of nuclei and chloroplasts of $mt^+$ and $mt^-$ cells, the zygotes become zygospores. It is notable that the young zygote shows uniparental inheritance of chloroplast DNA from the $mt^+$ parent and mitochondrial DNA from the $mt^-$ parent. Under the favorable conditions, the zygospores divide meiotically and germinate and then new haploid progenies, vegetative cells, are released.

• 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.