The nucleotide sequence of Syrian hamster HMG-CoA reductase cDNA.
The nucleotide sequence of Syrian hamster HMG-CoA reductase cDNA.
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叙利亚仓鼠 HMG-CoA 还原酶 cDNA 的核苷酸序列。
DOI：
10.1089/dna.1985.4.439
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发表时间：
1985
期刊：
影响因子：
--
通讯作者：
Simoni,RD
中科院分区：
文献类型：
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作者：
Skalnik,DG;Simoni,RD
我们测定了叙利亚仓鼠3-羟基-3-甲基戊二酰辅酶A（HMG-CoA）还原酶cDNA的核苷酸序列。比较推导的氨基酸序列与中国仓鼠的同源序列，揭示了高度保守的结构域，似乎具有功能意义。HMG-CoA还原酶的氨基端膜结构域具有100%同源性。该区域可以跨越内质网七次，并且被认为参与HMG-CoA还原酶的甾醇调节的降解（Gilet al.，1985; Liscumet等人，1985年）。羧基末端含有酶的活性位点，并表现出大于99%的同源性。连接这两个保守结构域的中心区域表现出更大的分歧。在该区域中，两个仓鼠系之间只有85%的同源性，表明该连接结构域具有不太严格的结构要求。
We have determined the nucleotide sequence of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase cDNA. Comparison of the deduced amino acid sequence with the homologous sequence from Chinese hamster reveals highly conserved domains which appear to have functional significance. The amino-terminal membrane domain of HMG-CoA reductase exhibits 100% homology. This region may span the endoplasmic reticulum seven times and is thought to be involved in the sterol-regulated degradation of HMG-CoA reductase (Gilet al., 1985; Liscumet al., 1985). The carboxyl terminus contains the active site of the enzyme and exhibits greater than 99% homology. A central region linking these two conserved domains exhibits greater divergence. In this region there is only 85% homology between the two hamster lines, suggesting that this linkage domain has a less stringent structural requirement.