The gtfT gene and its upstream region isolated from the Streptococcus sobrinus OMZ176 chromosomal DNA were sequenced. The gtfT gene was preceded by a potential Shine-Dalgarno sequence. The gtfT gene product, glucosyltransferase (GTF), displays a typical gram-positive bacterial signal peptide sequence and both an active site peptide sequence and carboxy-terminal repeats typical of GTFs. The signal sequence is similar to those of other known GTF proteins. The putative active-site peptide sequence of this enzyme was DGIRVDAVD, which was different by one amino acid from the active-site peptide sequence derived from two different types of the S. sobrinus GTFs reported previously (G. Mooser, S. A. Hefta, R. J. Paxton, J. E. Shively, and T. D. Lee, J. Biol. Chem. 266:8916-8922, 1991). The gtfT gene product has three repeated sequences of 51 to 52 amino acids and a partial repeat of 18 amino acids. Another open reading frame (ORF) was detected in the region immediately upstream of the gtfT gene. The upstream ORF showed substantial DNA homology with the gtfS gene isolated from Streptococcus downei MFe28. The inferred amino acid sequence of the upstream ORF has four repeating units and has extensive homology with the repeated peptides coded by the S. downei gtfS gene. These results suggested that the gtfT gene was a typical gtf gene isolated from the mutans streptococci and that the two gtf genes were located in tandem on the chromosomal DNA of S. sobrinus OMZ176.
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http://dx.doi.org/10.1128/iai.61.5.2096-2103.1993 | DOI Listing |
Planta
July 2016
Plant Pathology Laboratory, Faculty of Agriculture, Iwate University, Morioka, 020-8550, Japan.
Infection by apple latent spherical virus (ALSV) vectors that promote the expression of Arabidopsis thaliana FLOWERING LOCUS T ( AtFT ) or Gentiana triflora GtFT s accelerates flowering in gentian and lisianthus plants. Apple latent spherical virus (ALSV) has isometric virus particles (25 nm in diameter) that contain two ssRNA species (RNA1 and RNA2) and three capsid proteins (Vp25, Vp20, and Vp24). ALSV vectors are used for foreign gene expression and virus-induced gene silencing in a broad range of plant species.
View Article and Find Full Text PDFMicrobiol Immunol
May 2013
Department of Oral Microbiology, Nihon University School of Dentistry at Matsudo, Chiba 271-8587, Japan.
Two tandemly aligned glucosyltransferase (GTF) genes whose gene products are responsible for water-soluble glucan synthesis were isolated from Streptococcus dentirousetti NUM1303 and sequenced. One of the GTF genes of S. dentirousetti consisted of a 4110 bp open reading frame (ORF) that encoded for a 1369 amino acid protein and was revealed to be a S.
View Article and Find Full Text PDFBiochim Biophys Acta
February 2002
Department of Oral Science, National Institute of Infectious Diseases, 1-23-1 Toyama, Sinjuku-ku, Tokyo 162-8640, Japan.
Streptococcus sobrinus has four gtf genes, gtfI, gtfS, gtfT, and gtfU, on the chromosome. These genes correspond respectively to the enzymes GTF-I, GTF-S1, GTF-S2, and GTF-S3. An Escherichia coli MD66 clone that contained the S.
View Article and Find Full Text PDFMicrobiol Immunol
March 2001
Department of Microbiology, Okayama University Dental School, Okayama, Japan.
Two tandem genes encoding glucosyltransferase synthesizing water-soluble glucan (GTF-S) were cloned from the lambda gene library of Streptococcus cricetus HS-6 (serotype a) using anti-GTF-S antibody, and the nucleotide sequences were analyzed. The two genes (ORF1 and ORF2) were identified as streptococcal glucosyltransferases based on the following evidence: [1] the deduced amino acid sequences of their products have an active site for catalytic action and C-terminal repeated units for dextran binding, and [2] a homology search revealed that the ORF1 and ORF2 products are homologous to the GtfS protein (77.4%) of S.
View Article and Find Full Text PDFFEMS Immunol Med Microbiol
January 2000
Department of Microbiology, Nihon University School of Dentistry at Matsudo, Chiba, Japan.
A 1,3-alpha-glucan synthase (GTF-I), a highly branched 1, 6-alpha-glucan synthase (GTF-U) and a 1,6-alpha-glucan synthase (GTF-T) were purified to near homogeneity from the culture fluid of Streptococcus sobrinus strain B13N (serotype d) and characterized. In addition, a crude preparation of a recombinant oligo-isomaltosaccharide synthase (rGTF-S) was prepared from a cell-free extract of Escherichia coli MD124 transformant. Using four homogeneous GTF preparations including previously purified rGTF-S as antigens for immunization, 11 murine hybridomas producing a monoclonal antibody (MAb) were established through the fusion of myeloma cells (P3X63-Ag8-U1) and spleen cells of immunized BALB/c mice.
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