Functional conversion of the homologous proteins alpha-lactalbumin and lysozyme by exon exchange.
AUTOR(ES)
Kumagai, I
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=49402Documentos Relacionados
- Lactation is disrupted by alpha-lactalbumin deficiency and can be restored by human alpha-lactalbumin gene replacement in mice.
- Partial purification of rat alpha-lactalbumin mRNA.
- The construction, identification and characterisation of plasmids containing human alpha-lactalbumin cDNA sequences.
- alpha-Lactalbumin mRNA in 4-day lactating rat mammary gland.
- Efficient and specific ribozyme-mediated reduction of bovine alpha-lactalbumin expression in double transgenic mice.
