当前位置: X-MOL 学术Structure › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Programmed Trade-offs in Protein Folding Networks
Structure ( IF 5.7 ) Pub Date : 2020-10-13 , DOI: 10.1016/j.str.2020.09.009
Sebastian Pechmann 1
Affiliation  

Molecular chaperones as specialized protein quality control enzymes form the core of cellular protein homeostasis. How chaperones selectively interact with their substrate proteins thus allocate their overall limited capacity remains poorly understood. Here, I present an integrated analysis of sequence and structural determinants that define interactions of protein domains as the basic protein folding unit with the Saccharomyces cerevisiae Hsp70 Ssb. Structural homologs of single-domain proteins that differentially interact with Ssb for de novo folding were found to systematically differ in complexity of their folding landscapes, selective use of nonoptimal codons, and presence of short discriminative sequences, thus highlighting pervasive trade-offs in chaperone-assisted protein folding landscapes. However, short discriminative sequences were found to contribute by far the strongest signal toward explaining Ssb interactions. This observation suggested that some chaperone interactions may be directly programmed in the amino acid sequences rather than responding to folding challenges, possibly for regulatory advantages.



中文翻译:

蛋白质折叠网络中的程序化权衡

分子伴侣作为专门的蛋白质质量控​​制酶,构成了细胞蛋白质稳态的核心。分子伴侣如何选择性地与其底物蛋白相互作用,从而分配其整体有限的能力仍然知之甚少。在这里,我提出了序列和结构决定因素的综合分析,这些决定因素将蛋白质结构域的相互作用定义为与酿酒酵母Hsp70 Ssb的基本蛋白质折叠单位。与 Ssb从头差异相互作用的单域蛋白的结构同源物发现折叠在其折叠景观的复杂性、非最佳密码子的选择性使用和短判别序列的存在方面系统地不同,从而突出了分子伴侣辅助蛋白质折叠景观中普遍存在的权衡。然而,发现短的判别序列迄今为止对解释 Ssb 相互作用的信号最强。这一观察结果表明,一些分子伴侣相互作用可能直接在氨基酸序列中编程,而不是对折叠挑战做出反应,这可能是为了调节优势。

更新日期:2020-12-01
down
wechat
bug