Characterization of a signal peptide sequence in the cell-free translation product of sheep elastin mRNA.
Characterization of a signal peptide sequence in the cell-free translation product of sheep elastin mRNA.
复制标题
绵羊弹性蛋白 mRNA 无细胞翻译产物中信号肽序列的表征。
DOI:
10.1016/0003-9861(82)90317-4
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发表时间:
1982
影响因子:
3.9
通讯作者:
L. Sandberg
中科院分区:
文献类型:
--
作者:
J. Davidson;B. Leslie;T. Wolt;R. Crystal;L. Sandberg
In vitroexplant cultures of near-term sheep nuchal ligament secrete tropoelastin of approximateMr70,000–72,000 while the elastin cell-free product of sheep nuchal ligament RNA is 2000 to 3000Mrlarger. Automated Edman degradation of immunoprecipitates of radiolabeled cell-free elastin precursor demonstrated the presence of a 26-residue signal sequence which was absent from sheep tropoelastin secreted from explant cultures. In addition, a 20-residue overlap was established between the cell-free product and the secreted protein. This overlap region, representing the N-terminal sequence of ovine tropoelastin, demonstrated complete homology with the N-terminal sequence of porcine tropoelastin and near complete homology with chick tropoelastin. These findings suggest that cotranslational removal of this hydrophobic peptide extension is likely a correlate of vectorial transport of elastin into the secretory apparatus.