Analysis of a primer-independent GTF-I from Streptococcus salivarius.
A glucosyltransferase (GTF) gene, designated gtfL, from Streptococcus salivarius was cloned and expressed in Escherichia coli and its nucleotide sequence determined. The GTF-L enzyme catalysed the synthesis of water-insoluble glucan in a primer-independent manner. The nucleotide sequence and derived amino acid sequence of GTF-L were similar in size and domain structure to previously sequenced glucosyltransferases. However, a 464-bp region of high variability was identified which could be selectively amplified from strains of S. salivarius by the polymerase chain reaction and could therefore form the basis for species identification. No sequence-specific motifs related to the solubility and linkage of the glucan product or its need for a dextran primer could be ascertained.
Banas
J A
JA
Department of Microbiology, University of Oklahoma H.S.C., Oklahoma City 73190.
Simon
D
D
Williams
L K
LK
Ferretti
J J
JJ
Russell
R R
RR
D000595:Amino Acid Sequence; D001483:Base Sequence; D017124:Conserved Sequence; D005798:Genes, Bacterial / Q000235:genetics*; D005964:Glucosyltransferases / Q000235:genetics*; D008969:Molecular Sequence Data; D013045:Species Specificity; D013291:Streptococcus / Q000201:enzymology* / Q000235:genetics
D005964:Glucosyltransferases