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Sequence analysis of the Streptococcus mutans scrB gene.
1Department of Microbiology-Immunology, Northwestern University Medical-Dental Schools, Chicago, Illinois 60611.
Infection and Immunity
|August 1, 1988
Summary
The Streptococcus mutans scrB gene sequence was determined, revealing its sucrose-6-phosphate hydrolase enzyme. This enzyme shares similarities with Bacillus subtilis proteins, suggesting conserved functions in carbohydrate metabolism.
Area of Science:
- Microbiology
- Molecular Biology
- Enzymology
Background:
- Streptococcus mutans is a key bacterium in dental caries.
- Sucrose-6-phosphate hydrolase plays a role in carbohydrate metabolism.
- Understanding the genetic basis of enzyme function is crucial.
Purpose of the Study:
- To determine the complete nucleotide sequence of the Streptococcus mutans GS-5 scrB gene.
- To analyze the deduced amino acid sequence and properties of the encoded sucrose-6-phosphate hydrolase.
- To investigate potential homologies with related enzymes from other bacterial species.
Main Methods:
- DNA sequencing of the Streptococcus mutans GS-5 scrB gene.
- Bioinformatic analysis of nucleotide and deduced amino acid sequences.
- Comparison of sequence data with known enzyme databases.
Main Results:
- The complete nucleotide sequence of the scrB gene was elucidated.
- Promoter and ribosome-binding sites were identified upstream of the gene.
- The deduced enzyme has a molecular weight of 51,750, a pI of 5.9, and is hydrophilic.
- Significant homology was found with Bacillus subtilis sacA protein and other related enzymes.
Conclusions:
- The Streptococcus mutans scrB gene encodes sucrose-6-phosphate hydrolase with specific biochemical properties.
- Sequence homology suggests conserved functional domains and evolutionary relationships with other glycosyl hydrolases.
- This study provides a molecular basis for understanding sucrose metabolism in Streptococcus mutans.