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Structural models of the different trimers present in the core of phycobilisomes from Gracilaria chilensis based on crystal structures and sequences.

机译:基于晶体结构和序列,存在于来自江西的藻胆体核心中的不同三聚体的结构模型。

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摘要

Phycobilisomes (PBS) are accessory light harvesting protein complexes that directionally transfer energy towards photosystems. Phycobilisomes are organized in a central core and rods radiating from it. Components of phycobilisomes in Gracilaria chilensis (Gch) are Phycobiliproteins (PBPs), Phycoerythrin (PE), and Phycocyanin (PC) in the rods, while Allophycocyanin (APC) is found in the core, and linker proteins (L). The function of such complexes depends on the structure of each component and their interaction. The core of PBS from cyanobacteria is mainly composed by cylinders of trimers of alpha and beta subunits forming heterodimers of Allophycocyanin, and other components of the core including subunits alphaII and beta18. As for the linkers, Linker core (LC) and Linker core membrane (LCM) are essential for the final emission towards photoreaction centers. Since we have previously focused our studies on the rods of the PBS, in the present article we investigated the components of the core in the phycobilisome from the eukaryotic algae, Gracilaria chilensis and their organization into trimers. Transmission electron microscopy provided the information for a three cylinders core, while the three dimensional structure of Allophycocyanin purified from Gch was determined by X-ray diffraction method and the biological unit was determined as a trimer by size exclusion chromatography. The protein sequences of all the components of the core were obtained by sequencing the corresponding genes and their expression confirmed by transcriptomic analysis. These subunits have seldom been reported in red algae, but not in Gracilaria chilensis. The subunits not present in the crystallographic structure were modeled to build the different composition of trimers. This article proposes structural models for the different types of trimers present in the core of phycobilisomes of Gch as a first step towards the final model for energy transfer in this system.
机译:藻胆体(PBS)是辅助光收集蛋白复合物,可将能量定向转移至光系统。藻胆小体组织在中心核中并从其辐射出杆。棒Gra中藻胆体的成分是杆中的藻胆蛋白(PBPs),藻红蛋白(PE)和藻蓝蛋白(PC),而在核心中发现了别藻蓝蛋白(APC)和接头蛋白(L)。这种复合物的功能取决于每个组分的结构及其相互作用。来自蓝细菌的PBS的核心主要由形成别藻蓝蛋白异二聚体的α和β亚基的三聚体圆柱体组成,核心的其他成分包括亚基αII和β18。至于连接基,连接基核(LC)和连接基核膜(LCM)对于向光反应中心的最终发射至关重要。由于我们以前将研究重点放在了PBS的杆上,因此在本文中,我们研究了真核藻,江Gra(Gracilaria chilensis)藻胆体核心部分的组成及其三聚体的组织。透射电子显微镜提供了三个圆柱核的信息,而通过X射线衍射法确定了从Gch纯化的别花青素的三维结构,并通过尺寸排阻色谱法确定了其生物单元为三聚体。通过对相应基因进行测序,获得了核心所有成分的蛋白质序列,并通过转录组分析证实了它们的表达。很少在红藻中报道过这些亚基,但在智利江cil中却没有报道。对晶体结构中不存在的亚基进行建模,以建立三聚体的不同组成。本文提出了Gch藻胆体核心中存在的不同类型三聚体的结构模型,作为朝该系统中能量转移的最终模型迈出的第一步。

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