Regulation and Functional Complexity of the Chlorophyll-Binding Protein IsiA.

Regulation and Functional Complexity of the Chlorophyll-Binding Protein IsiA.
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叶绿素结合蛋白 IsiA 的调控和功能复杂性

DOI:
10.3389/fmicb.2021.774107
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发表时间:
2021
影响因子:
5.2
通讯作者:
Wang Q
Wang Q
中科院分区:
生物学2区
文献类型:
--
作者:
Jia A;Zheng Y;Chen H;Wang Q

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作为已知最古老的释氧光合作用生物,蓝藻在帮助塑造地球生态方面发挥着关键作用。铁是生物体系中氧化还原反应的理想过渡金属。蓝藻经常遇到缺铁问题,这是因为环境中的亚铁离子被氧化成在生理pH下高度不溶的铁离子。一系列的反应,包括光合膜的结构变化,使蓝藻能够经受住这种情况并保持光合作用。铁胁迫诱导蛋白A(ISIA)与蓝藻叶绿素(Chl)结合蛋白、光系统II核心天线蛋白CP43同源。在缺铁蓝藻中,ISIA是主要的含Chl蛋白,结合了这些细胞中高达50%的Chl,在铁缺乏的恢复过程中可以从ISIA中释放出来用于光系统的重建。由ISIA编码的色素-蛋白质复合体(CPVI-4)在近30年前被鉴定并在缺铁条件下表达。然而,其确切的功能尚不清楚,部分原因是其复杂的调控;ISIA的表达除了缺铁外,还受到各种类型的应激和异常生理状态的诱导。此外,ISIA形成了一系列执行不同功能的复合体。在这篇文章中,我们描述了在理解ISIA的调节和功能方面的进展,这是基于使用模型蓝藻的实验室研究。
As the oldest known lineage of oxygen-releasing photosynthetic organisms, cyanobacteria play the key roles in helping shaping the ecology of Earth. Iron is an ideal transition metal for redox reactions in biological systems. Cyanobacteria frequently encounter iron deficiency due to the environmental oxidation of ferrous ions to ferric ions, which are highly insoluble at physiological pH. A series of responses, including architectural changes to the photosynthetic membranes, allow cyanobacteria to withstand this condition and maintain photosynthesis. Iron-stress-induced protein A (IsiA) is homologous to the cyanobacterial chlorophyll (Chl)-binding protein, photosystem II core antenna protein CP43. IsiA is the major Chl-containing protein in iron-starved cyanobacteria, binding up to 50% of the Chl in these cells, and this Chl can be released from IsiA for the reconstruction of photosystems during the recovery from iron limitation. The pigment–protein complex (CPVI-4) encoded by isiA was identified and found to be expressed under iron-deficient conditions nearly 30years ago. However, its precise function is unknown, partially due to its complex regulation; isiA expression is induced by various types of stresses and abnormal physiological states besides iron deficiency. Furthermore, IsiA forms a range of complexes that perform different functions. In this article, we describe progress in understanding the regulation and functions of IsiA based on laboratory research using model cyanobacteria.
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