Isolation and characterization of the sucrose 6-phosphate hydrolase gene from Streptococcus mutans

@article{Hayakawa1986IsolationAC,
  title={Isolation and characterization of the sucrose 6-phosphate hydrolase gene from Streptococcus mutans},
  author={Mitsuo Hayakawa and Hiroyoshi Aoki and Howard K. Kuramitsu},
  journal={Infection and Immunity},
  year={1986},
  volume={53},
  pages={582 - 586}
}
The Streptococcus mutans GS-5 gene, scrB, coding for sucrose 6-phosphate hydrolase activity has been cloned into Escherichia coli utilizing the bacteriophage replacement vector lambda L47.1. DNA sequences containing the gene were initially subcloned into the moderate-copy-number plasmid vector pLG339 to yield active subclones. However, due to the instability of the resultant chimeric plasmids, the gene was subsequently subcloned into the low-copy-number vector pOU61 to yield the stable hybrid… 
Cloning and characterization of the scrA gene encoding the sucrose-specific Enzyme II of the phosphotransferase system from Staphylococcus xylosus
TLDR
The DNA sequence analysis of the scrA region revealed three open reading frames, one of which encodes a protein of 480 amino acids with significant similarity to sucrose-specific Enzymes 11 of phosphoenolpyruvate-dependent carbohydrate phosphotransferase systems (PTS).
Characterization and sequence analysis of the scrA gene encoding enzyme IIScr of the Streptococcus mutans phosphoenolpyruvate-dependent sucrose phosphotransferase system
TLDR
Results suggest that the sucrose PTS system of S. mutans is enzyme III independent, and this gene was located immediately upstream from the scrB gene and divergently transcribed from the opposite DNA strand.
Genetic analysis of scrA and scrB from Streptococcus sobrinus 6715.
TLDR
A DNA fragment containing scrA and scrB, which encode enzyme II of the phosphoenolpyruvate-dependent sucrose phosphotransferase system and sucrose-6-phosphate hydrolase, was isolated from a lambda gt10 genomic DNA library of Streptococcus sobrinus 6715 and suggested considerable divergence.
Isolation of DNA encoding sucrase genes from Streptococcus salivarius and partial characterization of the enzymes expressed in Escherichia coli
TLDR
Restriction enzyme fragments containing two sucrase genes have been isolated from a cosmid library of Streptococcus salivarius DNA and the properties of the enzymes were compared with those of previously characterized sucrases.
Biochemical and genetic analysis of Streptococcus mutans alpha-galactosidase.
TLDR
The aga gene coding for alpha-galactosidase in Streptococcus mutans was detected in a recombinant gene library constructed in phage lambda and indicated that the enzyme functions as a tetramer.
Regulation of Sucrose-6-Phosphate Hydrolase Activity inStreptococcus mutans: Characterization of thescrR Gene
TLDR
The results suggest that the scrR gene is involved in the regulation of scrB, and likely scrA, expression, and it is not clear whether sucrose acts as an inducer of expression of these genes or, alternatively, whether glucose and fructose act as repressors.
Transcriptional regulation of the Tn5276-located Lactococcus lactis sucrose operon and characterization of the sacA gene encoding sucrose-6-phosphate hydrolase.
TLDR
The Lactococcus lactis sucrose operon was located on the conjugative transposon Tn5276 and the nucleotide sequence of the sacA gene, encoding sucrose-6-phosphate hydrolase, and its surrounding regions was determined and it was confirmed that transcription is initiated at two Sucrose-inducible promoters with a back-to-back organization.
Molecular cloning and characterization of the spaB gene of Streptococcus sobrinus.
TLDR
It is shown that the rSpaB protein has physico-chemical and antigenic identity with the S. sobrinus SpaB protein, the presence of cross-reactive proteins in the extracellular protein of serotypes a and d of the mutans group of streptococci and that the SpaBprotein is expressed on the surface of mutans streptitiscal serotype a, d and g.
Sequence analysis of the Streptococcus mutans scrB gene
TLDR
The complete nucleotide sequence of the Streptococcus mutans GS-5 scrB gene coding for sucrose-6-phosphate hydrolase activity was determined and showed significant homology with those of the sacA protein from Bacillus subtilis.
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