类 Bestrophin 蛋白 4 参与了衣藻光合作用对光照波动的适应。

IF 6.5 1区 生物学 Q1 PLANT SCIENCES
Liat Adler, Chun Sing Lau, Kashif M Shaikh, Kim A van Maldegem, Alex L Payne-Dwyer, Cecile Lefoulon, Philipp Girr, Nicky Atkinson, James Barrett, Tom Z Emrich-Mills, Emilija Dukic, Michael R Blatt, Mark C Leake, Gilles Peltier, Cornelia Spetea, Adrien Burlacot, Alistair J McCormick, Luke C M Mackinder, Charlotte E Walker
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引用次数: 0

摘要

在许多真核藻类中,Rubisco 的二氧化碳固定作用通过一种二氧化碳浓缩机制得到加强,该机制利用了一种富含 Rubisco 的细胞器(称为类肾蕊管)。拟肾小管由称为拟肾小管的类木质膜网络穿过,拟肾小管被认为是输送二氧化碳的通道。在模式藻类衣藻(Chlamydomonas reinhardtii)中,拟肾小管被一种类似bestrophin的跨膜蛋白BST4拴在Rubisco基质上。在这里,我们发现 BST4 形成了一个定位于焦磷酸小管的复合物。BST4积累受损的衣藻突变体(bst4)形成了正常的类肾小管,而在拟南芥(Arabidopsis thaliana)中异源表达BST4并不会导致类肾小管并入重组的Rubisco缩合物中。衣藻 bst4 突变体在空气二氧化碳水平下的连续光照条件下没有表现出生长受损,但在波动光照条件下生长受损。通过量化叶绿素荧光的非光化学淬灭(NPQ),我们提出,与对照品系相比,bst4 在从暗到光的转变过程中,叶绿体内腔 pH 值会短暂降低。我们的结论是,BST4 不是一种系链蛋白,而很可能是一种参与腔内离子平衡的肾小管离子通道,在光波动期间具有特别重要的作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Bestrophin-like protein 4 is involved in photosynthetic acclimation to light fluctuations in Chlamydomonas.

In many eukaryotic algae, CO2 fixation by Rubisco is enhanced by a CO2-concentrating mechanism, which utilizes a Rubisco-rich organelle called the pyrenoid. The pyrenoid is traversed by a network of thylakoid membranes called pyrenoid tubules, which are proposed to deliver CO2. In the model alga Chlamydomonas (Chlamydomonas reinhardtii), the pyrenoid tubules have been proposed to be tethered to the Rubisco matrix by a bestrophin-like transmembrane protein, BST4. Here, we show that BST4 forms a complex that localizes to the pyrenoid tubules. A Chlamydomonas mutant impaired in the accumulation of BST4 (bst4) formed normal pyrenoid tubules, and heterologous expression of BST4 in Arabidopsis (Arabidopsis thaliana) did not lead to the incorporation of thylakoids into a reconstituted Rubisco condensate. Chlamydomonas bst4 mutants did not show impaired growth under continuous light at air level CO2 but were impaired in their growth under fluctuating light. By quantifying the non-photochemical quenching (NPQ) of chlorophyll fluorescence, we propose that bst4 has a transiently lower thylakoid lumenal pH during dark-to-light transition compared to control strains. We conclude that BST4 is not a tethering protein but is most likely a pyrenoid tubule ion channel involved in the ion homeostasis of the lumen with particular importance during light fluctuations.

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来源期刊
Plant Physiology
Plant Physiology 生物-植物科学
CiteScore
12.20
自引率
5.40%
发文量
535
审稿时长
2.3 months
期刊介绍: Plant Physiology® is a distinguished and highly respected journal with a rich history dating back to its establishment in 1926. It stands as a leading international publication in the field of plant biology, covering a comprehensive range of topics from the molecular and structural aspects of plant life to systems biology and ecophysiology. Recognized as the most highly cited journal in plant sciences, Plant Physiology® is a testament to its commitment to excellence and the dissemination of groundbreaking research. As the official publication of the American Society of Plant Biologists, Plant Physiology® upholds rigorous peer-review standards, ensuring that the scientific community receives the highest quality research. The journal releases 12 issues annually, providing a steady stream of new findings and insights to its readership.
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