通过外显子交换实现同源蛋白α-乳白蛋白和溶菌酶的功能转换。
Functional conversion of the homologous proteins alpha-lactalbumin and lysozyme by exon exchange.
作者信息
Kumagai I, Takeda S, Miura K
机构信息
Department of Industrial Chemistry, Faculty of Engineering, University of Tokyo, Japan.
出版信息
Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):5887-91. doi: 10.1073/pnas.89.13.5887.
Exons of eukaryotic genes that encode proteins frequently appear to encode structural and/or functional protein units [Gilbert, W. (1978) Nature (London) 271, 501; Blake, C.C.F. (1979) Nature (London) 277, 598]. alpha-Lactalbumin and c-type lysozyme are functionally quite different but structurally highly homologous proteins. Their gene organizations have been shown to be virtually the same and their exon structures are identical. The exon 2 region of hen lysozyme contains most of the amino acid residues that make up its catalytic cleft. In this study, we engineered a hybrid protein in which the exon 2 region of goat alpha-lactalbumin was replaced with that of hen lysozyme. This conferred catalytic activity on the alpha-lactalbumin, which is a nonenzymatic protein in its native structural form.
编码蛋白质的真核基因外显子常常似乎编码结构和/或功能蛋白质单元[吉尔伯特，W.（1978年）《自然》（伦敦）271, 501；布莱克，C.C.F.（1979年）《自然》（伦敦）277, 598]。α-乳白蛋白和c型溶菌酶在功能上差异很大，但在结构上高度同源。它们的基因组织已被证明几乎相同，并且它们的外显子结构是一样的。母鸡溶菌酶的外显子2区域包含构成其催化裂隙的大部分氨基酸残基。在本研究中，我们构建了一种杂合蛋白，其中山羊α-乳白蛋白的外显子2区域被母鸡溶菌酶的外显子2区域所取代。这赋予了α-乳白蛋白催化活性，而α-乳白蛋白在其天然结构形式下是一种非酶蛋白。
Zotero 插件