Literature DB >> 8371114

Sequence of the gtfK gene of Streptococcus salivarius ATCC 25975 and evolution of the gtf genes of oral streptococci.

P M Giffard1, D M Allen, C P Milward, C L Simpson, N A Jacques.   

Abstract

Many strains of oral streptococci secrete glucosyltransferases (GTFs) that polymerize sucrose into glucans that form an integral part of the plaque matrix on the tooth surface. Recently, we reported the cloning of two closely linked GTF-encoding genes (gtfJ and gtfK) from Streptococcus salivarius ATCC 25975 as well as the sequence of gtfJ, which encodes a primer-dependent GTF that synthesizes an insoluble product (a GTF-I). In this communication we report the sequence of gtfK, which encodes a primer-dependent GTF that synthesizes a soluble product (a GTF-S), as well as the sequence of a small downstream open reading frame of unknown function. The deduced sequence of GtfK was compared with those of seven other streptococcal Gtfs and an unrooted phylogenetic tree constructed. This analysis suggested that Gtfs with similar product specificities do not form phylogenetic clusters and was consistent with currently accepted phylogenetic schemes. The tree was tested by constructing a series of 'sub-trees' from different blocks of the alignment. Evidence was obtained for recombination events involving gtfB and gtfC from S. mutans GS-5, gtfJ and gtfK from S. salivarius, as well as the gtfI genes from S. downei and S. sobrinus. The recombination events between gtfB and gtfC, and between the two gtfI genes, were confirmed by examining divergences at silent sites.

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Year:  1993        PMID: 8371114     DOI: 10.1099/00221287-139-7-1511

Source DB:  PubMed          Journal:  J Gen Microbiol        ISSN: 0022-1287


  10 in total

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3.  Streptococcus salivarius ATCC 25975 possesses at least two genes coding for primer-independent glucosyltransferases.

Authors:  C L Simpson; P M Giffard; N A Jacques
Journal:  Infect Immun       Date:  1995-02       Impact factor: 3.441

4.  Structural Insights into the Carbohydrate Binding Ability of an α-(1→2) Branching Sucrase from Glycoside Hydrolase Family 70.

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8.  Identification of amino acid residues in Streptococcus mutans glucosyltransferases influencing the structure of the glucan product.

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  10 in total

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