源自互补DNA的雄激素依赖性精囊腺蛋白VI的结构。

Structure of the androgen dependent SVS VI protein as derived from cDNA.

作者信息

Schifman A L, Mansson P E, Carter D B, Yamada K, Harris M M, Harris S E

机构信息

W. Alton Jones Cell Science Center, Inc., Lake Placid, NY 12946.

出版信息

Mol Cell Endocrinol. 1988 Sep;59(1-2):57-65. doi: 10.1016/0303-7207(88)90195-5.

DOI:10.1016/0303-7207(88)90195-5

PMID:2848738

Abstract

The 11S poly(A+)RNA from rat seminal vesicle was cloned. By hybrid selection of clones reacting to the low molecular weight region of the 11S peak, a clone containing a new seminal vesicle cDNA sequence called SVS VI was isolated. The DNA sequence of two overlapping cDNAs (pSV24 and pSV33) is presented. The sequence of SVS VI was compared to the previously isolated SVS IV and SVS V cDNAS. Dot hybridization showed that SVS VI is androgen responsive after giving testosterone to castrated rats. The hydrophilicity was analyzed using standard Bionet procedures. All three proteins are extremely variable, rich in alpha-helix and very water soluble. The computer predicted hydrophilicity is compared for SVS VI, V and IV. A small region in the 3'-non-coding area of SVS VI has high similarity to a region in SVS IV mRNA.

摘要

对来自大鼠精囊的11S多聚腺苷酸（A+）RNA进行了克隆。通过对与11S峰低分子量区域反应的克隆进行杂交筛选，分离出一个包含名为SVS VI的新精囊cDNA序列的克隆。给出了两个重叠cDNA（pSV24和pSV33）的DNA序列。将SVS VI的序列与先前分离的SVS IV和SVS V cDNA进行了比较。点杂交显示，给去势大鼠注射睾酮后，SVS VI对雄激素有反应。使用标准的生物网络程序分析了亲水性。所有三种蛋白质都极具变异性，富含α-螺旋且极易溶于水。对SVS VI、V和IV的计算机预测亲水性进行了比较。SVS VI 3'非编码区的一个小区域与SVS IV mRNA中的一个区域具有高度相似性。