Key Laboratory of Forest Tree Genetic Improvement and Biotechnology, Ministry of Education, Northeast Forestry University, Harbin, China.
Published: January 2011
AI Article Synopsis
Article Abstract
In this study we initiated a proteomic investigation of the maize thylakoid membrane by using a shotgun proteomic approach based on LC-MS(E). A total of 34 maize thylakoid membrane proteins were identified, the majority of which are primarily involved in photosynthesis, including the light-reaction and carbon assimilation. It is noteworthy that all of the core subunits of the Photosystem II were identified in our search. Proteins involved in other processes, such as iron storage, were also detected in our study. The quantity of each identified protein was also determined. Of interest, we discovered that the amount of the three ATP synthase subunits were not equivalent, suggesting that these proteins perform other functions in addition to ATP synthesis. To our knowledge this is the first extensive proteomic investigation of the maize thylakoid membrane, and will likely enable further study of maize photosynthesis and chloroplast development.
School of Chemistry and Environment, Guangdong Ocean University, Zhanjiang, 524088, China; Analyzing and Testing Center, Guangdong Ocean University, Zhanjiang, 524088, China; Analytical and Testing Center for Ocean in Western of Guangdong Province, Guangdong Provincial Observation and Research Station for Tropical Ocean Environment in Western Coastal Water, Guangdong Ocean University, Zhanjiang, 524088, China. Electronic address:
The plant thylakoid membrane hosting the light-harvesting complex (LHCII) is the site of oxygenic photosynthesis. Contrary to the earlier consensus of a protein-driven single lamellar phase of the thylakoid, despite containing 40% non-bilayer-forming lipids, recent experiments confirm the polymorphic state of the functional thylakoid. What, then, is the origin of this polymorphism and what factors control it? The current Letter addresses the question using a total of 617.
Tianjin Institute of Industrial Biotechnology Chinese Academy of Sciences, Institute of Biotechnology, West 7th Avenue 32, Tianjin Airport Economic Area, 300308, 300308, Tianjin, CHINA.
Nature produces ATP, the energy currency, by converting solar energy (photophosphorylation) and chemical energy (substrate-level phosphorylation and oxidative phosphorylation). Green electricity, as a significant and sustainable energy carrier, plays a crucial role in achieving a carbon-neutral society. In this work, we established and verified a novel electrodriven phosphorylation method.
The thermoacidophilic red alga Cyanidioschyzon merolae survives its challenging environment likely in part by operating a carbon-concentrating mechanism (CCM). Here, we demonstrated that C. merolae's cellular affinity for CO2 is stronger than the affinity of its rubisco for CO2.
The Arabidopsis (Arabidopsis thaliana) yellow variegated2 (var2) mutant, lacking functional FILAMENTATION TEMPERATURE-SENSITIVE H2 (FtsH2), an ATP-dependent zinc metalloprotease, is a powerful tool for studying the photosystem II (PSII) repair process in plants. FtsH2, forming hetero-hexamers with FtsH1, FtsH5, and FtsH8, plays an indispensable role in PSII proteostasis. Although abiotic stresses like cold and heat increase chloroplast reactive oxygen species (ROS) and PSII damage, var2 mutants behave like wild-type plants under heat stress but collapse under cold stress.
