Energizing the light harvesting antenna: Insight from CP29

被引:13
|
作者
Ioannidis, Nikolaos E. [1 ]
Papadatos, Sotiris [1 ]
Daskalakis, Vangelis [1 ]
机构
[1] Cyprus Univ Technol, Dept Environm Sci & Technol, POB 50329, Limassol, Cyprus
来源
关键词
Photosystem II; Antenna proteins; Photoprotection; Non photochemical quenching; Proton motive force; PHOTOPROTECTIVE ENERGY-DISSIPATION; PHOTOSYSTEM-II; MEMBRANE-PROTEINS; FORCE-FIELD; COMPLEX; ZEAXANTHIN; DYNAMICS; BINDING; PLANTS; LHCII;
D O I
10.1016/j.bbabio.2016.07.005
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
How do plants cope with excess light energy? Crop health and stress tolerance are governed by molecular photoprotective mechanisms. Protective exciton quenching in plants is activated by membrane energization, via unclear conformational changes in proteins called antennas. Here we show that pH and salt gradients stimulate the response of such an antenna under low and high energization by all-atom Molecular Dynamics Simulations. Novel insight establishes that helix-5 (H5) conformation in CP29 from spinach is regulated by chemiosmotic factors. This is selectively correlated with the chl-614 macrocycle deformation and interactions with nearby pigments, that could suggest a role in plant photoprotection. Adding to the significance of our findings, H5 domain is conserved among five antennas (LHCB1-5). These results suggest that light harvesting complexes of Photosystem II, one of the most abundant proteins on earth, can sense chemiosmotic gradients via their H5 domains in an upgraded role from a solar detector to also a chemiosmotic sensor. (C) 2016 Elsevier B.V. All rights reserved.
引用
收藏
页码:1643 / 1650
页数:8
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