体内实验证明麦芽糖结合蛋白与SecB的相互作用由动力学分配决定。
Demonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioning.
作者信息
Khisty V J, Randall L L
机构信息
Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660, USA.
出版信息
J Bacteriol. 1995 Jun;177(11):3277-82. doi: 10.1128/jb.177.11.3277-3282.1995.
Abstract
An early step in the export of maltose-binding protein to the periplasm is interaction with the molecular chaperone SecB. We demonstrate that binding to SecB in vivo is determined by a kinetic partitioning between the folding of maltose-binding protein to its native state and its association with SecB. A complex of SecB and a species of maltose-binding protein that folds slowly is shown to be longer-lived than a complex of the wild-type maltose-binding protein and SecB. In addition, we show that incomplete nascent chains, which are unable to fold, remain complexed with SecB.
摘要
麦芽糖结合蛋白输出到周质的早期步骤是与分子伴侣SecB相互作用。我们证明，在体内与SecB的结合取决于麦芽糖结合蛋白折叠成其天然状态与其与SecB结合之间的动力学分配。SecB与折叠缓慢的麦芽糖结合蛋白物种形成的复合物显示比野生型麦芽糖结合蛋白和SecB形成的复合物寿命更长。此外，我们表明，无法折叠的不完全新生链仍与SecB复合。
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