Isolation of a yeast protein kinase gene by screening with a mammalian protein kinase cDNA.

Isolation of a yeast protein kinase gene by screening with a mammalian protein kinase cDNA.
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通过用哺乳动物蛋白激酶 cDNA 筛选来分离酵母蛋白激酶基因。

DOI:
10.1089/dna.1.1988.7.469
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发表时间:
1988
期刊:
DNA (Mary Ann Liebert, Inc.)
影响因子:
--
通讯作者:
Maurer,RA
Maurer,RA
中科院分区:
--
文献类型:
--
作者:
Maurer,RA

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通过与牛 cAMP 依赖性蛋白激酶催化亚基的克隆 cDNA 杂交,鉴定并分离了新的酿酒酵母蛋白激酶基因。这种新分离的酵母基因编码一种 680 个氨基酸的蛋白质,与几种丝氨酸/苏氨酸蛋白激酶显示出很强的序列相似性。蛋白激酶催化结构域位于蛋白质的羧基末端部分。大的氨基末端结构域与任何已知的蛋白激酶没有序列相似性。氨基末端结构域似乎可能介导新鉴定的酵母蛋白激酶的未知调节剂的作用。
The gene for a newSaccharomyces cerevisiaeprotein kinase was identified and isolated by hybridization to a cloned cDNA for the catalytic subunit of bovine cAMP-dependent protein kinase. This newly isolated yeast gene encodes a 680-amino-acid protein that shows strong sequence similarity to several serine/threonine protein kinases. The protein kinase catalytic domain is located at the carboxy-terminal portion of the protein. A large, amino-terminal domain shows no sequence similarity to any known protein kinase. It seems likely that the amino-terminal domain mediates the effects of an unknown regulator of the newly identified yeast protein kinase.