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藻胆蛋白的进化分析:对其结构与功能关系的启示

Evolutionary analysis of phycobiliproteins: implications for their structural and functional relationships.

作者信息

Zhao Fangqing, Qin Song

机构信息

Institute of Oceanology, Chinese Academy of Sciences, Qingdao, China.

出版信息

J Mol Evol. 2006 Sep;63(3):330-40. doi: 10.1007/s00239-005-0026-2. Epub 2006 Jul 7.

Abstract

Phycobiliproteins, together with linker polypeptides and various chromophores, are basic building blocks of phycobilisomes, a supramolecular complex with a light-harvesting function in cyanobacteria and red algae. Previous studies suggest that the different types of phycobiliproteins and the linker polypeptides originated from the same ancestor. Here we retrieve the phycobilisome-related genes from the well-annotated and even unfinished cyanobacteria genomes and find that many sites with elevated d(N)/d(S) ratios in different phycobiliprotein lineages are located in the chromophore-binding domain and the helical hairpin domains (X and Y). Covariation analyses also reveal that these sites are significantly correlated, showing strong evidence of the functional-structural importance of interactions among these residues. The potential selective pressure driving the diversification of phycobiliproteins may be related to the phycobiliprotein-chromophore microenvironment formation and the subunits interaction. Sites and genes identified here would provide targets for further research on the structural-functional role of these residues and energy transfer through the chromophores.

摘要

藻胆蛋白与连接多肽及各种发色团一起,是藻胆体的基本组成部分,藻胆体是一种在蓝细菌和红藻中具有捕光功能的超分子复合物。先前的研究表明,不同类型的藻胆蛋白和连接多肽起源于同一个祖先。在这里,我们从注释完善甚至尚未完成的蓝细菌基因组中检索出与藻胆体相关的基因,发现不同藻胆蛋白谱系中许多d(N)/d(S)比率升高的位点位于发色团结合结构域和螺旋发夹结构域(X和Y)。共变分析还表明,这些位点显著相关,有力证明了这些残基之间相互作用在功能结构上的重要性。驱动藻胆蛋白多样化的潜在选择压力可能与藻胆蛋白 - 发色团微环境的形成以及亚基相互作用有关。这里鉴定出的位点和基因将为进一步研究这些残基的结构功能作用以及通过发色团的能量转移提供靶点。

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