Cloning and nucleotide sequence of the bglA gene from Erwinia herbicola and expression of beta-glucosidase activity in Escherichia coli.
Genomic DNA fragments encoding beta-glucosidase activity from the wild-type strain WD4 of Erwinia herbicola were cloned into Escherichia coli. Two clones containing a common fragment encoded a polypeptide of 58,000 Da. Cloned beta-glucosidase, expressed in E. coli, showed activity against natural beta-glucoside sugars except for cellobiose. An open reading frame of 1442 bp termed bglA was identified by nucleotide sequencing and it coded for a protein of 480 amino acids (M(r) 53,896) which showed significant homology with beta-glucosidases from glycosyl hydrolase family 1.
Marri
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Dipartimento di Biologia Molecolare, Università di Siena, Italy.
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Venditti
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D003001:Cloning, Molecular; D004885:Erwinia / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D015971:Gene Expression Regulation, Enzymologic; D005798:Genes, Bacterial / Q000235:genetics*; D005822:Genetic Vectors; D008969:Molecular Sequence Data; D001617:beta-Glucosidase / Q000096:biosynthesis / Q000235:genetics*
D001617:beta-Glucosidase