SecB与核糖体结合的多肽的结合特性与它与全长变性蛋白的结合特性相同。
Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins.
作者信息
Randall L L, Topping T B, Hardy S J, Pavlov M Y, Freistroffer D V, Ehrenberg M
机构信息
Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660, USA.
出版信息
Proc Natl Acad Sci U S A. 1997 Feb 4;94(3):802-7. doi: 10.1073/pnas.94.3.802.
Abstract
The interaction of the chaperone SecB with ribosome-bound polypeptides that are in the process of elongation has been studied using an in vitro protein synthesis system. The binding is characterized by the same properties as those demonstrated for the binding of SecB to full-length proteins that are in nonnative conformation: it is readily reversible and has no specificity for the leader peptide. In addition, it is shown that the growing polypeptide chains must achieve a critical length to bind tightly enough to allow their isolation in complex with SecB. This explains the longstanding observation that, even when export is cotranslational, it begins late in synthesis. Furthermore, the required length is approximately the same as the length that defines the binding frame within denatured, full-length proteins bound to SecB.
摘要
利用体外蛋白质合成系统，对伴侣蛋白SecB与处于延伸过程中的核糖体结合多肽之间的相互作用进行了研究。这种结合具有与SecB与非天然构象的全长蛋白质结合所表现出的相同特性：它很容易逆转，并且对前导肽没有特异性。此外，研究表明，正在生长的多肽链必须达到一个临界长度，才能紧密结合，从而能够与SecB形成复合物进行分离。这解释了长期以来的一个观察结果，即即使转运是共翻译的，它也在合成后期才开始。此外，所需的长度与定义与SecB结合的变性全长蛋白质内结合框架的长度大致相同。
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