Change in the photochemical and structural organization of thylakoids from pea (Pisum sativum) under salt stress

类囊体 光合作用 豌豆 叶绿素荧光 化学 电子传输链 生物物理学 光系统II 光化学 光系统I 光合反应中心 光系统 700页 叶绿素 叶绿体 生物 生物化学 基因 有机化学
作者
Kunal Dhokne,Jayendra Pandey,Ranay Mohan Yadav,Pavithra Ramachandran,Jyoti Ranjan Rath,Rajagopal Subramanyam
出处
期刊:Plant Physiology and Biochemistry [Elsevier BV]
卷期号:177: 46-60 被引量:21
标识
DOI:10.1016/j.plaphy.2022.02.004
摘要

Salt can induce adverse effects, primarily on the photosynthetic process, ultimately influencing plant productivity. Still, the impact of salt on the photosynthesis process in terms of supercomplexes organization of thylakoid structure and function is not understood in Pea (Pisum sativum). To understand the structure and function in the leaves and thylakoids under salt (NaCl) treatment, we used various biophysical and biochemical techniques like infrared gas analyzer, chlorophyll a fluorescence, circular dichroism, electron microscopy, blue native gels, and western blots. The net photosynthetic rate, transpiration rate, and stomatal conductance were reduced significantly, whereas the water use efficiency was enhanced remarkably under high salt conditions (200 mM NaCl). The photochemical efficiency of both photosystem (PS) I and II was reduced in high salt by inhibiting their donor and acceptor sides. Interestingly the non-photochemical quenching (NPQ) is reduced in high salt; however, the non-regulated energy dissipation (NO) of PSII increased, leading to inactivation of PSII. The obtained results exhibit inhibition of NAD(P)H dehydrogenase (NDH) mediated pathway-dependent cyclic electron transport under salinity caused a decrease in proton motive force of ΔpH and Δψ. Further, the electron micrographs show the disorganization of grana thylakoids under salt stress. Furthermore, the macro-organization and supercomplexes of thylakoids were significantly affected by high salt. Specifically, the mega complexes, PSII-LHCII, PSI-LHCI, and NDH complexes were notably reduced, ultimately altering the electron transport. The reaction center proteins of oxygen-evolving complexes, D1 and D2 proteins were affected to high salt indicating changes in photochemical activities.
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