Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification.

Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification.
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DOI:
10.1007/s11120-021-00891-7
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发表时间:
2022-06
影响因子:
3.7
通讯作者:
Nowaczyk, Marc M.
Nowaczyk, Marc M.
中科院分区:
生物学3区
文献类型:
--
作者:
Lambertz, Jan;Liauw, Pasqual;Whitelegge, Julian P.;Nowaczyk, Marc M.

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组装像光系统II(PSII)这样的大的、多辅助因子的膜蛋白复合体需要高度的协调。这一过程是由一个庞大的辅助蛋白网络推动的,这些辅助蛋白瞬时结合到未组装的亚基、预组装的模块或PSII的中间状态,这些亚基由亚基的子集组成。然而,这些未成熟的、部分组装的PSII复合体的分析受到其低丰度和内在不稳定性的阻碍。本研究通过Twin Strep-tag CP43从嗜热蓝细菌长链球菌体中分离纯化PSII,并通过离子交换层析将其进一步分离成成熟和未成熟的复合体。对未成熟的Psb27-PSII中间体的质谱分析显示,有六种不同的Psb27蛋白形式具有不同的脂质修饰。对类囊体脂蛋白的成熟和功能作用进行了讨论。
The assembly of large, multi-cofactor membrane protein complexes like photosystem II (PSII) requires a high level of coordination. The process is facilitated by a large network of auxiliary proteins that bind transiently to unassembled subunits, preassembled modules or intermediate states of PSII, which are comprised of a subset of subunits. However, analysis of these immature, partially assembled PSII complexes is hampered by their low abundance and intrinsic instability. In this study, PSII was purified from the thermophilic cyanobacterium Thermosynechococcus elongatus via Twin-Strep-tagged CP43 and further separated by ion exchange chromatography into mature and immature complexes. Mass spectrometry analysis of the immature Psb27-PSII intermediate revealed six different Psb27 proteoforms with distinct lipid modifications. The maturation and functional role of thylakoid localized lipoproteins are discussed.
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