THE GENERAL CONCEPT OF MOLECULAR CHAPERONES

THE GENERAL CONCEPT OF MOLECULAR CHAPERONES
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DOI:
10.1098/rstb.1993.0023
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发表时间:
1993-03-29
期刊:
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES
影响因子:
--
通讯作者:
ELLIS, RJ
ELLIS, RJ
中科院分区:
其他
文献类型:
--
作者:
ELLIS, RJ

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这篇介绍性的文章提出了一个概念框架,在这个框架中考虑正在出现的关于蛋白质的信息,称为分子伴侣,并提出了一些在这个新的生物化学领域可能有用的定义。分子伴侣目前在功能上被定义为一类不相关的蛋白质家族,它们帮助体内其他含有多肽的结构正确地以非共价方式组装,但当它们执行正常的生物学功能时,它们不是这些组装结构的组成部分。这个定义中的术语组装不仅包括新合成的多肽的折叠和可能发生的任何缔合成低聚物,还包括当蛋白质执行其功能、跨膜运输或在诸如热休克等压力后修复或破坏时可能发生的折叠或缔合程度的任何变化。已知的分子伴侣不传递正确组装所必需的空间信息,但似乎通过与相互作用的蛋白质表面结合来发挥作用,这些相互作用在各种细胞过程中短暂暴露;这种结合抑制了错误的相互作用,否则可能产生非功能结构。因此,分子伴侣的概念并不与蛋白质自组装的原理相矛盾,而是通过提出在体内的自组装需要其他蛋白质分子的帮助来限定它。
This introductory article proposes a conceptual framework in which to consider the information that is emerging about the proteins called molecular chaperones, and suggests some definitions that may be useful in this new field of biochemistry. Molecular chaperones are currently defined in functional terms as a class of unrelated families of protein that assist the correct non-covalent assembly of other polypeptide-containing structures in vivo, but which are not components of these assembled structures when they are performing their normal biological functions. The term assembly in this definition embraces not only the folding of newly synthesized polypeptides and any association into oligomers that may occur, but also includes any changes in the degree of either folding or association that may take place when proteins carry out their functions, are transported across membranes, or are repaired or destroyed after stresses such as heat shock. Known molecular chaperones do not convey steric information essential for correct assembly, but appear to act by binding to interactive protein surfaces that are transiently exposed during various cellular processes; this binding inhibits incorrect interactions that may otherwise produce non-functional structures. Thus the concept of molecular chaperones doe not contradict the principle of protein self-assembly, but qualifies it by suggesting that in vivo self-assembly requires assistance by other protein molecules.