Anderson L K, Toole C M
Department of Biological Science, University of Tulsa, 600 S. College Ave, Tulsa, OK 74104, USA.
Mol Microbiol. 1998 Nov;30(3):467-74. doi: 10.1046/j.1365-2958.1998.01081.x.
Biological self-assembly is remarkable in its fidelity and in the efficient production of intricate molecular machines and functional materials from a heterogeneous mixture of macromolecules. The phycobilisome, a light-harvesting structure of cyanobacteria, presents the opportunity to study an in vivo assembly process in detail. The phycobilisome molecular architecture is defined, and crystal structures are available for all major proteins, as are a large sequence database (including a genome sequence) and effective genetic systems exist for some cyanobacteria. Recent studies on subunit interaction, covalent modification, and protein stability suggest a model for the earliest events in the phycobilisome assembly pathway. Partitioning of phycobilisome proteins between degradation and assembly is proposed to be controlled by the interaction equilibria between phycobilisome assembly partners, processing enzymes and chaperones. The model provides plausible explanations for existing observations and makes predictions that are amenable to direct experimental investigation.
生物自组装在保真度以及从大分子异质混合物高效生产复杂分子机器和功能材料方面表现出色。藻胆体是蓝细菌的一种光捕获结构，为详细研究体内组装过程提供了契机。藻胆体的分子结构已明确，所有主要蛋白质的晶体结构均可获取，同时还有一个大型序列数据库（包括基因组序列），并且一些蓝细菌拥有有效的遗传系统。近期关于亚基相互作用、共价修饰和蛋白质稳定性的研究提出了藻胆体组装途径中最早事件的模型。藻胆体蛋白质在降解和组装之间的分配被认为受藻胆体组装伙伴、加工酶和伴侣之间的相互作用平衡控制。该模型为现有观察结果提供了合理的解释，并做出了适合直接实验研究的预测。
