Molecular cloning of a cDNA encoding the glycoprotein of hen oviduct microsomal signal peptidase.
Molecular cloning of a cDNA encoding the glycoprotein of hen oviduct microsomal signal peptidase.
复制标题
编码母鸡输卵管微粒体信号肽酶糖蛋白的 cDNA 的分子克隆。
DOI：
10.1042/bj2820447
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发表时间：
1992
期刊：
影响因子：
--
通讯作者：
Lively,MO
中科院分区：
文献类型：
--
作者：
Newsome,AL;McLean,JW;Lively,MO
Detergent-solubilized hen oviduct signal peptidase has been characterized previously as an apparent complex of a 19 kDa protein and a 23 kDa glycoprotein (GP23) [Baker & Lively (1987) Biochemistry 26, 8561-8567]. A cDNA clone encoding GP23 from a chicken oviduct lambda gt11 cDNA library has now been characterized. The cDNA encodes a protein of 180 amino acid residues with a single site for asparagine-linked glycosylation that has been directly identified by amino acid sequence analysis of a tryptic-digest peptide containing the glycosylated site. Immunoblot analysis reveals cross-reactivity with a dog pancreas protein. Comparison of the deduced amino acid sequence of GP23 with the 22/23 kDa glycoprotein of dog microsomal signal peptidase [Shelness, Kanwar & Blobel (1988) J. Biol. Chem. 263, 17063-17070], one of five proteins associated with this enzyme, reveals that the amino acid sequences are 90% identical. Thus the signal peptidase glycoprotein is as highly conserved as the sequences of cytochromes c and b from these same species and is likely to be found in a similar form in many, if not all, vertebrate species. The data also show conclusively that the dog and avian signal peptidases have at least one protein subunit in common.
