Transmembrane β-barrels: Evolution, folding and energetics.

Transmembrane β-barrels: Evolution, folding and energetics.
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DOI:
10.1016/j.bbamem.2017.09.020
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发表时间:
2017-12
期刊:
Biochimica et biophysica acta. Biomembranes
影响因子:
--
通讯作者:
Mahalakshmi R
Mahalakshmi R
中科院分区:
其他
文献类型:
--
作者:
Chaturvedi D;Mahalakshmi R

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跨膜β-桶(外膜蛋白,或OMP)的生物发生是新生多肽与易位酶、桶组装机制和辅助分子伴侣蛋白的精心设计的多步骤协调。存在几种理论描述了分子伴侣辅助的OMP体内组装和体外无辅助(自发)折叠的机制。在结构上,细菌来源的OMP具有偶数股,而线粒体β桶是偶数和奇数股。原核生物和真核生物的β-桶和它们的折叠机制之间有几个潜在的相似之处,但它们在进化起源上的联系尚不清楚。虽然OMP在序列和功能上表现出多样性,但它们具有相似的生物物理属性和结构。类似地,理解复杂的OMP组装机制是重要的,特别是在已经进化为执行更复杂功能的真核β-桶中。在这里,我们讨论了已知的β-桶的进化,折叠和稳定性方面,并试图突出β-桶生物发生和蛋白质稳定的突出问题。
The biogenesis of transmembrane β-barrels (outer membrane proteins, or OMPs) is an elaborate multistep orchestration of the nascent polypeptide with translocases, barrel assembly machinery, and helper chaperone proteins. Several theories exist that describe the mechanism of chaperone-assisted OMP assembly in vivo and unassisted (spontaneous) folding in vitro. Structurally, OMPs of bacterial origin possess even-numbered strands, while mitochondrial β-barrels are even- and odd-stranded. Several underlying similarities between prokaryotic and eukaryotic β-barrels and their folding machinery are known; yet, the link in their evolutionary origin is unclear. While OMPs exhibit diversity in sequence and function, they share similar biophysical attributes and structure. Similarly, it is important to understand the intricate OMP assembly mechanism, particularly in eukaryotic β-barrels that have evolved to perform more complex functions. Here, we deliberate known facets of β-barrel evolution, folding, and stability, and attempt to highlight outstanding questions in β-barrel biogenesis and proteostasis.
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