编码叶酰聚（γ-谷氨酸）合成酶的人cDNA的表达克隆及其一级结构的测定。
Expression cloning of a human cDNA encoding folylpoly(gamma-glutamate) synthetase and determination of its primary structure.
作者信息
Garrow T A, Admon A, Shane B
机构信息
Department of Nutritional Sciences, University of California, Berkeley 94720.
出版信息
Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9151-5. doi: 10.1073/pnas.89.19.9151.
Abstract
A human cDNA for folypoly(gamma-glutamate) synthetase [FPGS; tetrahydrofolate:L-glutamate gamma-ligase (ADP forming), EC 6.3.2.17] has been cloned by functional complementation of an Escherichia coli folC mutant. The cDNA encodes a 545-residue protein of M(r) 60,128. The deduced sequence has regions that are highly homologous to peptide sequences obtained from purified pig liver FPGS and shows limited homology to the E. coli and Lactobacillus casei FPGSs. Expression of the cDNA in E. coli results in elevated expression of an enzyme with characteristics of mammalian FPGS. Expression of the cDNA in AUXB1, a mammalian cell lacking FPGS activity, overcomes the cell's requirement for thymidine and purines but does not overcome the cell's glycine auxotrophy, consistent with expression of the protein in the cytosol but not the mitochondria.
摘要
通过大肠杆菌folC突变体的功能互补克隆了人叶酸聚（γ-谷氨酸）合成酶[FPGS；四氢叶酸：L-谷氨酸γ-连接酶（形成ADP），EC 6.3.2.17]的cDNA。该cDNA编码一个545个氨基酸残基、分子量为60128的蛋白质。推导的序列具有与从纯化的猪肝FPGS获得的肽序列高度同源的区域，并且与大肠杆菌和干酪乳杆菌的FPGS具有有限的同源性。该cDNA在大肠杆菌中的表达导致具有哺乳动物FPGS特征的酶的表达升高。该cDNA在缺乏FPGS活性的哺乳动物细胞AUXB1中的表达克服了细胞对胸苷和嘌呤的需求，但没有克服细胞的甘氨酸营养缺陷，这与该蛋白在细胞质而非线粒体中的表达一致。
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