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小鼠L-组氨酸脱羧酶74-kDa形式通过其羧基末端序列进行膜靶向和结合。

Membrane targeting and binding of the 74-kDa form of mouse L-histidine decarboxylase via its carboxyl-terminal sequence.

作者信息

Suzuki S, Tanaka S, Nemoto K, Ichikawa A

机构信息

Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.

出版信息

FEBS Lett. 1998 Oct 16;437(1-2):44-8. doi: 10.1016/s0014-5793(98)01195-8.

DOI:10.1016/s0014-5793(98)01195-8
PMID:9804169
Abstract

The role of the C-terminal region of the 74-kDa form of L-histidine decarboxylase (HDC) in the targeting to the endoplasmic reticulum (ER) was investigated in COS-7 cells. The deletion of a 10-kDa segment (residues 578-662) of the C-terminal end of HDC, especially a 20 amino acid sequence (residues 588-607), abrogated the targeting to the ER. The C-terminal 10-kDa portion is sufficient to target the green fluorescent protein (GFP) to the ER. The 74-kDa form of HDC synthesized in an in vitro translation system post-translationally associated with the heterogeneous canine microsomal membranes. These results suggest that the C-terminal 10-kDa portion of HDC contains a signal necessary for HDC to be targeted to the ER membrane.

摘要

在COS-7细胞中研究了L-组氨酸脱羧酶(HDC)74-kDa形式的C末端区域在靶向内质网(ER)中的作用。删除HDC C末端的一个10-kDa片段(第578-662位氨基酸),尤其是一个20个氨基酸的序列(第588-607位氨基酸),会消除其向内质网的靶向作用。C末端的10-kDa部分足以将绿色荧光蛋白(GFP)靶向内质网。在体外翻译系统中合成的74-kDa形式的HDC在翻译后与异源犬微粒体膜结合。这些结果表明,HDC的C末端10-kDa部分包含HDC靶向内质网的必要信号。

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