Ditz Noah, Braun Hans-Peter, Eubel Holger
Department of Plant Proteomics, Institute of Plant Genetics, Leibniz Universität Hannover, Hannover, Germany.
Front Plant Sci. 2024 Aug 16;15:1380969. doi: 10.3389/fpls.2024.1380969. eCollection 2024.
Equipped with a photosynthetic apparatus that uses the energy of solar radiation to fuel biosynthesis of organic compounds, chloroplasts are the metabolic factories of mature leaf cells. The first steps of energy conversion are catalyzed by a collection of protein complexes, which can dynamically interact with each other for optimizing metabolic efficiency under changing environmental conditions.
For a deeper insight into the organization of protein assemblies and their roles in chloroplast adaption to changing environmental conditions, an improved complexome profiling protocol employing a MS-cleavable cross-linker is used to stabilize labile protein assemblies during the organelle isolation procedure.
Changes in protein:protein interaction patterns of chloroplast proteins in response to four different light intensities are reported. High molecular mass assemblies of central chloroplast electron transfer chain components as well as the PSII repair machinery react to different light intensities. In addition, the chloroplast encoded RNA-polymerase complex was found to migrate at a molecular mass of ~8 MDa, well above its previously reported molecular mass. Complexome profiling data produced during the course of this study can be interrogated by interested readers via a web-based online resource (https://complexomemap.de/projectsinteraction-chloroplasts).
叶绿体配备有光合装置,利用太阳辐射能为有机化合物的生物合成提供能量,是成熟叶细胞的代谢工厂。能量转换的第一步由一系列蛋白质复合物催化,这些复合物可在不断变化的环境条件下动态相互作用,以优化代谢效率。
为了更深入地了解蛋白质组装体的组织及其在叶绿体适应环境变化中的作用,采用一种改进的复合物组分析方案,该方案使用可被质谱裂解的交联剂,在细胞器分离过程中稳定不稳定的蛋白质组装体。
报道了叶绿体蛋白的蛋白质-蛋白质相互作用模式在四种不同光照强度下的变化。叶绿体中心电子传递链成分以及PSII修复机制的高分子量组装体对不同光照强度有反应。此外,发现叶绿体编码的RNA聚合酶复合物的迁移分子量约为8 MDa,远高于先前报道的分子量。本研究过程中产生的复合物组分析数据可供感兴趣的读者通过基于网络的在线资源(https://complexomemap.de/projectsinteraction-chloroplasts)查询。