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Evolutionary history of ATP‐binding cassette proteins
FEBS Letters ( IF 3.0 ) Pub Date : 2020-11-21 , DOI: 10.1002/1873-3468.13985
Sriram Srikant 1
Affiliation  

ATP‐binding cassette (ABC) proteins are found in every sequenced genome and evolved deep in the phylogenetic tree of life. ABC proteins form one of the largest homologous protein families, with most being involved in substrate transport across biological membranes, and a few cytoplasmic members regulating in essential processes like translation. The predominant ABC protein classification scheme is derived from human members, but the increasing number of fully sequenced genomes permits to reevaluate this paradigm in the light of the evolutionary history the ABC‐protein superfamily. As we study the diversity of substrates, mechanisms, and physiological roles of ABC proteins, knowledge of the evolutionary relationships highlights similarities and differences that can be attributed to specific branches in protein divergence. While alignments and trees built on natural sequence variation account for the evolutionary divergence of ABC proteins, high‐throughput experiments and next‐generation sequencing creating experimental sequence variation are instrumental in identifying functional constraints. The combination of natural and experimentally produced sequence variation allows a broader and more rational study of the function and physiological roles of ABC proteins.

中文翻译:

ATP结合盒蛋白的进化史

ATP 结合盒 (ABC) 蛋白存在于每个测序的基因组中,并在生命的系统发育树中进化。ABC 蛋白形成了最大的同源蛋白家族之一,大多数参与跨生物膜的底物转运,少数细胞质成员在翻译等基本过程中进行调节。主要的 ABC 蛋白质分类方案来自人类成员,但越来越多的完全测序的基因组允许根据 ABC 蛋白质超家族的进化历史重新评估这一范式。当我们研究 ABC 蛋白质的底物、机制和生理作用的多样性时,进化关系的知识突出了可归因于蛋白质分歧中特定分支的异同。虽然建立在自然序列变异上的比对和树解释了 ABC 蛋白的进化差异,但高通量实验和下一代测序创建实验序列变异有助于识别功能限制。自然和实验产生的序列变异的结合允许对 ABC 蛋白的功能和生理作用进行更广泛和更合理的研究。
更新日期:2020-11-21
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