Literature DB >> 2976010

Sequence analysis of the gtfC gene from Streptococcus mutans GS-5.

S Ueda1, T Shiroza, H K Kuramitsu.   

Abstract

The nucleotide sequence of the gtfC gene, which codes for glucosyltransferase synthesizing both water-soluble and water-insoluble glucans, and its flanking regions from Streptococcus mutans GS-5, was determined. Although the gtfC gene (4218 bp) is preceded by a Shine-Dalgarno (SD) sequence, a promoter-like sequence for this gene could not be identified. The gtfC gene product composed of 1375 amino acid residues (approx. 153 kDa) is generally hydrophilic with three small hydrophobic domains. Two direct repeating units were found near the C terminus of the peptide. The gtfC gene has extensive homology with the previously sequenced gtfB gene. The homologous regions correspond to the signal sequence, an internal region, and the direct repeating units of the peptide. An open reading frame preceded by an SD sequence and followed by an inverted repeat sequence was found immediately downstream from the gtfC gene. The combined sequences of the gtfB and gtfC genes as well as flanking regions suggest that the two gtf genes and the small downstream coding region could be coordinately expressed within an operon. The possible evolution of the gtfC gene in S. mutans GS-5 is also discussed.

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Year:  1988        PMID: 2976010     DOI: 10.1016/0378-1119(88)90382-4

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  61 in total

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8.  Immunological characteristics of a synthetic peptide associated with a catalytic domain of mutans streptococcal glucosyltransferase.

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9.  Construction of a model secretion system for oral streptococci.

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10.  Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with alpha-(1-->4) and alpha-(1-->6) glucosidic bonds.

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Journal:  Appl Environ Microbiol       Date:  2002-09       Impact factor: 4.792

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