Cloning of a Streptococcus mutans glucosyltransferase gene coding for insoluble glucan synthesis

@article{Aoki1986CloningOA,
  title={Cloning of a Streptococcus mutans glucosyltransferase gene coding for insoluble glucan synthesis},
  author={Hiroyoshi Aoki and Teruaki Shiroza and Mitsuo Hayakawa and S I Sato and Howard K. Kuramitsu},
  journal={Infection and Immunity},
  year={1986},
  volume={53},
  pages={587 - 594}
}
The gtfB gene coding for a glucosyltransferase (GTF) activity of Streptococcus mutans GS-5 was isolated on a 15.4-kilobase DNA fragment by using a lambda L47.1 gene library. The activity was catalyzed by gene products of 150 and 145 kilodaltons which reacted with antibodies directed against both soluble and insoluble glucan-synthesizing GTFs. The enzyme present in crude Escherichia coli extracts synthesized both soluble and insoluble glucans. The enzyme was partially purified from lysates of… 
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Nucleotide sequence of the Streptococcus mutans gtfD gene encoding the glucosyltransferase-S enzyme.
TLDR
Results indicate that both the Streptococcus mutans GS-5 gtfD and GTF-S genes evolved from a common ancestral gene.
Peptide sequences for sucrose splitting and glucan binding within Streptococcus sobrinus glucosyltransferase (water-insoluble glucan synthetase)
TLDR
The gene encoding glucosyltransferase responsible for water-insoluble glucan synthesis (GTF-I) of Streptococcus sobrinus was cloned, expressed, and sequenced and the primary structure of the GTF-I peptide was found to be very similar to that of the homologous protein from another strain of S.Sobrinus.
Functional Analyses of a Conserved Region in Glucosyltransferases of Streptococcus mutans
TLDR
Results confirmed the report from another laboratory that Asp residues in the Gtf-P1 region are essential for enzymatic catalysis and provide new evidence that identical residues may function differently in closely related GTF enzymes.
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References

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Expression of a Streptococcus mutans glucosyltransferase gene in Escherichia coli
TLDR
Chromosomal DNA from Streptococcus mutans strain UAB90 (serotype c) was cloned into Escherichia coli K-12 and the gtfA protein appears to be present in S. mutans cells of serotypes c, e, and f, and a cross-reacting protein was made by serotype b cells.
Isolation and characterization of a fructosyltransferase gene from Streptococcus mutans GS-5
TLDR
A comparison of the properties of the cloned enzyme with those previously characterized from another serotype c S. mutans strain suggests that multiple FTF genes may be present in these organisms.
Cloned gtfA gene of Streptococcus mutans LM7 alters glucan synthesis in Streptococcus sanguis
TLDR
The cloned S. mutans LM7 gene was closely related to the gtfA gene cloned by Robeson et al. and may play a role in glucan synthesis by interacting with extant high-molecular-weight glucosyltransferases.
Insoluble glucan synthesis by Streptococcus mutans serotype c strains
TLDR
Dextransucrase and mutansynthetase appear to be distinct enzymes, since the latter possesses a higher molecular weight (155,000 compared to 140,000), a much lower isoelectric point, and did not cross-react with antibody directed against dextransucase.
Isolation and characterization of an extracellular glucosyltransferase synthesizing insoluble glucan from Streptococcus mutans serotype c
A glucosyltransferase which synthesized insoluble glucan in polyacrylamide gel was isolated from the culture supernatant of Streptococcus mutans Ingbritt (serotype c) by ultrafiltration, ethanol
Immunological relationships between glucosyltransferases from Streptococcus mutans serotypes
TLDR
Antibody prepared against the homogeneous soluble glucan-synthesizing enzyme demonstrated similar effects to the anti-GTF-B fraction, but this antibody fraction did not strongly inhibit either the cell-associated glycosyltransferase activity or cellular adherence of any of the four strains.
Purification and properties of glucosyltransferase responsible for water-insoluble glucan synthesis from Streptococcus mutans
TLDR
Analysis of the structure of water-insoluble glucan indicated that the enzyme catalyzed the formation of branch points in alpha-1,6-glucan (dextran) and transferred the glucosyl moiety of sucrose to the C-3 position of the branching glucose residue of dextran.
Characterization of extracellular glucosyltransferase activity of Steptococcus mutans
TLDR
The extracellular glycosyltransferase activity of Sterptococcus mutans GS-5 has been resolved into two non-overlapping fractions after gel filtration chromatography on Bio Gel A-15 columns and the glucosyltransferases in both fractions are discussed in terms of the role of the enzymes in both soluble and insoluble glucan formation.
Mapping of a cloned glucosyltransferase gene in Streptococcus mutans
TLDR
A cloned glucosyltransferase (gtfA) fragment was used in transformation experiments to determine the genetic location of gftA on the Streptococcus mutans chromosome, and results indicate that S. mutans genes can be mapped by this procedure.
Expression of Streptococcus mutans aspartate-semialdehyde dehydrogenase gene cloned into plasmid pBR322.
TLDR
It was seen that the orientation of the S. mutans DNA fragment inserted into the promotor region of the pBR322 tetracycline resistance (Tcr) gene affected expression of Tcr, and affected the stability of the plasmid in certain E. coli strains.
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