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酵母高尔基体t-SNARE Sed5蛋白的蛋白质-蛋白质相互作用,与其神经质膜同源物 syntaxin 1不同。

Protein-protein interactions of the yeast Golgi t-SNARE Sed5 protein distinct from its neural plasma membrane cognate syntaxin 1.

作者信息

Kosodo Y, Noda Y, Yoda K

机构信息

Department of Biotechnology, University of Tokyo, Japan.

出版信息

Biochem Biophys Res Commun. 1998 Sep 18;250(2):212-6. doi: 10.1006/bbrc.1998.9288.

Abstract

Targeting of vesicles to the acceptor membrane in protein transport depends on membrane proteins called SNAREs. Saccharomyces cerevisiae Golgi t-SNARE Sed5 protein and its neural cognate syntaxin 1 have similar three alpha-helices which are predicted to form coiled coils. We dissected the helices of Sed5 and found several characteristics unexpectedly distinct from those of syntaxin 1. Most importantly, only the N-terminal helix is responsible for the binding of Sly1 protein while almost the entire molecule of syntaxin is necessary for the binding of the cognate, Munc-18. The N-terminal region of Sed5 protein also binds to the C-terminal helix and Sly1 protein interfered this binding.

摘要

在蛋白质运输过程中,囊泡与受体膜的靶向作用取决于一种名为SNARE的膜蛋白。酿酒酵母高尔基体t-SNARE Sed5蛋白及其神经同源物 syntaxin 1具有相似的三个α螺旋,预计会形成卷曲螺旋。我们剖析了Sed5的螺旋结构,发现了一些与syntaxin 1出乎意料的不同特征。最重要的是,只有N端螺旋负责与Sly1蛋白结合,而syntaxin几乎整个分子对于同源物Munc-18的结合都是必需的。Sed5蛋白的N端区域也与C端螺旋结合,而Sly1蛋白会干扰这种结合。

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