Types | DnaRegion
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Roles | CDS
Coding
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Sequences | BBa_K531004_sequence (Version 1)
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Description
DspB comes from the bacteria Actinobacillus actinomycetemcomitansis. It is most likely an N-acetylglucosaminidase that causes the detachment of cells from biofilm colonies through the 1→ 4 glycosidic bond of β-substituted N-acetylglucosamine. DspB is homologous to family 20 glycosyl hydrolases which cleave terminal monosaccharide residues.
Notes
The WT gene has a low GC content ~40%. Caulobacter crescentus is GC rich and prefers a high GC content. Therefore, we optimized the GC content by comparing the codons in the wild type dspB gene to their corresponding amino acid codons that are most expressed in Caulobacter.
We also eliminated the stop codon at the end of dspB because we wanted to add another gene to it that also needed to be transcribed.
Source
Kaplan, J., Ragunath, C., Ramasubbu, N., and Fine, D. Detachment of Actinobacillus actinomycetemcomitans Biofilm Cells by an Endogenous beta-Hexosaminidase Activity. Journal of Bacteriology. 2003 August; 185(16): 4693-4698.