衣藻细胞的高效循环电子流和功能超配合物

Pierre Joliot, Julien Sellés, Françis-André Wollman, André Verméglio
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引用次数: 0

摘要

在厌氧条件下,在完整的莱茵衣藻细胞中,在存在甲基紫藻(MV)的情况下,在PSI周围的循环电子流(CEF)速率非常高(在最低介质中分别为180 s-1或210s-1)。甲基紫紫素存在时,CEF效率低下的观察结果与Asada等人先前在破碎叶绿体(Plant CellPhysiol)中报道的结果一致。31(4)(1990) 557-564)。通过对P700和PC吸光度变化的分析,我们提出了2个PC分子、1个PSI和1个cytb6f之间对应于一个功能性超络合物的约束是这些高CEF率的原因。在没有甲基紫蛋白的情况下也观察到超络合物的形成,但其最大CEF速率较低(约100 s-1),这表明该化合物促进了电子从PSI受体转移到cytb6f基质侧的中介。对状态转换有缺陷的衣原体突变体的CEF的进一步分析表明,需要激酶驱动过渡到状态2才能建立这种功能性超复合体结构。然而,LHCII天线的运动并不参与这一过程。我们讨论了辅助蛋白的可能参与,其中包括一种小细胞6f相关的多肽,PETO蛋白,它是STT7激酶的靶标之一。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
High efficient cyclic electron flow and functional supercomplexes in Chlamydomonas cells
A very high rate for cyclic electron flow (CEF) around PSI (~180 s-1 or 210 s-1 in minimum medium or in the presence of a carbon source respectively) is measured in the presence of methyl viologen (MV) in intact cells of Chlamydomonas reinhardtii under anaerobic conditions. The observation of an efficient CEF in the presence of methyl viologen is in agreement with the previous results reports of Asada et al in broken chloroplasts (Plant Cell Physiol. 31(4) (1990) 557-564). From the analysis of the P700 and PC absorbance changes, we propose that a confinement between 2 PC molecules, 1 PSI and 1 cytb6f corresponding to a functional supercomplex is responsible for these high rates of CEF. Supercomplex formation is also observed in the absence of methyl viologen, but with lower maximal CEF rate (about 100 s-1) suggesting that this compound facilitates the mediation of electron transfer from PSI acceptors to the stromal side of cytb6f. Further analysis of CEF in mutants of Chlamydomonas defective in state transitions shows the requirement of a kinase-driven transition to state 2 to establish this functional supercomplex configuration. However, a movement of the LHCII antennae is not involved in this process. We discuss the possible involvement of auxiliary proteins, among which is a small cytb6f-associated polypeptide, the PETO protein, which is one of the targets of the STT7 kinase.
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