Farnesylation of Batten disease CLN3 protein.
Farnesylation of Batten disease CLN3 protein.
复制标题
Batten 病 CLN3 蛋白的法尼基化。
DOI：
10.1055/s-2007-973665
复制
发表时间：
1997
期刊：
影响因子：
1.4
通讯作者：
Morris,GN
中科院分区：
文献类型：
--
作者：
Pullarkat,RK;Morris,GN
Batten病CLN3基因蛋白的预测氨基酸序列的羧基末端是CQLS。预计该基序是半胱氨酸残基处法尼基化的位点。为了确定这是否确实是法尼基化的，我们已经使用来自牛脑的法尼基转移酶制剂进行了四肽CVLS、CAIL和CQLS的体外异戊烯化。数据显示，CQLS是类似于CVLS的法尼基的良好受体，而它是不像CAIL的香叶基香叶基的不良受体，CAIL是香叶基香叶基的良好受体。这表明CLN3基因产物可能是法尼基化蛋白。
The carboxyl terminal of the predicted amino acid sequence of the Batten disease CLN3 gene protein is CQLS. This motif is expected to be a site for farnesylation at the cysteine residue. In order to determine whether this is indeed farnesylated we have carried out the in-vitro prenylation of tetrapeptides CVLS, CAIL and CQLS using a farnesyl transferase preparation from bovine brain. The data shows that the CQLS is a good acceptor of a farnesyl group similar to CVLS while it is a poor acceptor of a geranylgeranyl group unlike CAIL, which is a good acceptor of a geranylgeranyl group. This suggests that the CLN3 gene product may be a farnesylated protein.