Cloning and sequencing of liver cDNA coding for bovine protein C.
Cloning and sequencing of liver cDNA coding for bovine protein C.
复制标题
编码牛蛋白 C 的肝脏 cDNA 的克隆和测序。
DOI：
10.1073/pnas.81.18.5653
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发表时间：
1984
影响因子：
11.1
通讯作者：
R. MacGillivray
中科院分区：
文献类型：
--
作者：
G. Long;R. Belagaje;R. MacGillivray
从牛肝脏文库中克隆了编码蛋白C的基因，并测定了其序列。两个重叠的克隆编码成熟蛋白的整个轻链和重链，以及一个以前未报道的连接二肽(Lys-Arg)和一个39个氨基酸的前导肽区域。克隆的鉴定和特征确定了肝脏是蛋白C生物合成的场所。一个连续的编码区表明，一个单链前体蛋白被制造出来，在有限的蛋白质分解后产生成熟的轻链和重链。天冬氨酸的密码子位于轻链氨基酸的第71位，表明存在于成熟蛋白质这一位置的β-羟基天冬氨酸是天冬氨酸残基翻译后修饰的结果。与其他维生素K依赖的凝血因子在轻链氨基末端区域的氨基酸序列同源性继续进入前导肽区域。
cDNA coding for protein C has been cloned from a bovine liver library in plasmid vector pBR322 and its sequence has been determined. Two overlapping clones code for the entire light and heavy chains of the mature protein, as well as a previously unreported connecting dipeptide (Lys-Arg) and a 39-amino acid leader peptide region. Identification and characterization of the clones establishes the liver as a site of protein C biosynthesis. A contiguous coding region reveals that a one-chain precursor protein is made that upon limited proteolysis yields both the mature light and heavy chains. The codon for aspartic acid is found at light chain amino acid position 71, showing that the beta-hydroxyaspartic acid that exists in this position of the mature protein is the result of post-translational modification of an aspartic acid residue. Amino acid sequence homology in the amino-terminal region of the light chain with other vitamin K-dependent coagulation factors is continued into the leader peptide region.