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https://www.readbyqxmd.com/read/26483802/ros-mediated-enhanced-transcription-of-cyp38-promotes-the-plant-tolerance-to-high-light-stress-by-suppressing-gtpase-activation-of-psbo2
#1
Yongqiang Wang, Lizhang Zeng, Da Xing
As a member of the Immunophilin family, cyclophilin38 (CYP38) is discovered to be localized in the thylakoid lumen, and is reported to be a participant in the function regulation of thylakoid membrane protein. However, the molecule mechanisms remain unclear. We found that, CYP38 plays an important role in the process of regulating and protecting the plant to resist high light (HL) stress. Under HL condition, the gene expression of CYP38 is enhanced, and if CYP38 gene is deficient, photochemistry efficiency, and chlorophyll content falls distinctly, and excessive reactive oxygen species synthesis occurs in the chloroplast...
2015: Frontiers in Plant Science
https://www.readbyqxmd.com/read/25639878/proteomic-and-metabolic-profiles-of-cakile-maritima-scop-sea-rocket-grown-in-the-presence-of-cadmium
#2
Manel Taamalli, Angelo D'Alessandro, Cristina Marrocco, Federica Gevi, Anna Maria Timperio, Lello Zolla
Recent physiological reports have documented how Cakile maritima Scop. Sea Rocket could accumulate high doses of Cd without altering its physiological parameters. In the present study, we performed an integrated proteomics (2DE) and metabolomics (HPLC-MS) investigation to determine the molecular mechanisms underlying cadmium (Cd) tolerance of this halophyte. Peculiar features were observed: (i) up-regulation of thiol compound anabolism, including glutathione and phytochelatin homeostasis, which allows an intracellular chelation of Cd and its compartmentalization into vacuole by a significant up-regulation of vacuolar transporters; (ii) up-regulation of the PPP and Calvin cycle (both at the enzyme and metabolite level), which utterly promoted the maintenance of NADPH/NADP(+) homeostasis, other than the accumulation of triose-phosphates (serving as anabolic intermediates for triacylglycerol biosynthesis) and the glyoxylate precursor phosphoglycolate, to promote photorespiration and consequently CO2 release...
April 2015: Molecular BioSystems
https://www.readbyqxmd.com/read/25605904/psb27-a-thylakoid-protein-enabling-arabidopsis-to-adapt-to-changing-light-intensity
#3
Xin Hou, Aigen Fu, Veder J Garcia, Bob B Buchanan, Sheng Luan
In earlier studies we have identified FKBP20-2 and CYP38 as soluble proteins of the chloroplast thylakoid lumen that are required for the formation of photosystem II supercomplexes (PSII SCs). Subsequent work has identified another potential candidate functional in SC formation (PSB27). We have followed up on this possibility and isolated mutants defective in the PSB27 gene. In addition to lack of PSII SCs, mutant plants were severely stunted when cultivated with light of variable intensity. The stunted growth was associated with lower PSII efficiency and defective starch accumulation...
February 3, 2015: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/22706283/crystal-structure-of-arabidopsis-cyclophilin38-reveals-a-previously-uncharacterized-immunophilin-fold-and-a-possible-autoinhibitory-mechanism
#4
Dileep Vasudevan, Aigen Fu, Sheng Luan, Kunchithapadam Swaminathan
Cyclophilin38 (CYP38) is one of the highly divergent cyclophilins from Arabidopsis thaliana. Here, we report the crystal structure of the At-CYP38 protein (residues 83 to 437 of 437 amino acids) at 2.39-Å resolution. The structure reveals two distinct domains: an N-terminal helical bundle and a C-terminal cyclophilin β-barrel, connected by an acidic loop. Two N-terminal β-strands become part of the C-terminal cyclophilin β-barrel, thereby making a previously undiscovered domain organization. This study shows that CYP38 does not possess peptidyl-prolyl cis/trans isomerase activity and identifies a possible interaction of CYP38 with the E-loop of chlorophyll protein47 (CP47), a component of photosystem II...
June 2012: Plant Cell
https://www.readbyqxmd.com/read/17909185/a-chloroplast-cyclophilin-functions-in-the-assembly-and-maintenance-of-photosystem-ii-in-arabidopsis-thaliana
#5
Aigen Fu, Zengyong He, Hye Sun Cho, Amparo Lima, Bob B Buchanan, Sheng Luan
Photosynthetic light reactions rely on the proper function of large protein complexes (including photosystems I and II) that reside in the thylakoid membrane. Although their composition, structure, and function are known, the repertoire of assembly and maintenance factors is still being determined. Here we show that an immunophilin of the cyclophilin type, CYP38, plays a critical role in the assembly and maintenance of photosystem II (PSII) supercomplexes (SCs) in Arabidopsis. Mutant plants with the CYP38 gene interrupted by T-DNA insertion showed stunted growth and were hypersensitive to high light...
October 2, 2007: Proceedings of the National Academy of Sciences of the United States of America
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