The carboxyl terminal domain of Streptococcus mutans glucosyltransferases prevents secretion in Escherichia coli.
The extracellular glucosyltransferases (GTFs) of Streptococcus mutans are not secreted into the periplasmic space of Escherichia coli when the corresponding gtf genes are isolated in the latter organism. The utilization of both deletion analysis and gtfB: phoA fusions indicate that the signal sequences of the GTFs are functional in E. coli. However, these results further suggest that amino acid sequences present in the carboxyl terminus of the GTFs inhibit secretion through the cytoplasmic membrane in E. coli.
Kato
C
C
Department of Pediatric Dentistry, University of Texas Health Science Center, San Antonio 78284.
Kuramitsu
H K
HK
D000469:Alkaline Phosphatase / Q000032:analysis; D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology*; D005964:Glucosyltransferases / Q000235:genetics / Q000502:physiology*; D013295:Streptococcus mutans / Q000201:enzymology*
C036655:1,3-alpha-D-glucan synthase; D005964:Glucosyltransferases; D000469:Alkaline Phosphatase