Functional conversion of the homologous proteins alpha-lactalbumin and lysozyme by exon exchange.
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.
Kumagai
I
I
Department of Industrial Chemistry, Faculty of Engineering, University of Tokyo, Japan.
Takeda
S
S
Miura
K
K
D000818:Animals; D001483:Base Sequence; D002645:Chickens; D005091:Exons; D006041:Goats; D007768:Lactalbumin / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D009113:Muramidase / Q000235:genetics* / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D011993:Recombinant Fusion Proteins; D013379:Substrate Specificity
D009838:Oligodeoxyribonucleotides; D011993:Recombinant Fusion Proteins; D007768:Lactalbumin; D009113:Muramidase