Molecular basis for the association of glucosyltransferases with the cell surface of oral streptococci.
The expression of Streptococcus mutans mutant glucosyltransferase-I enzymes in S. sanguis and S. milleri suggests that cell-associated glucosyltransferase activity is dependent upon both glucan synthesis and glucan binding by the carboxyl-terminal repeating units of the enzyme. Mutant enzymes lacking these repeating units were only present in the extracellular fluids of these transformed streptococcal strains.
Kato
C
C
Department of Microbiology, University of Texas Health Science Center, San Antonio.
Kuramitsu
H K
HK
D015153:Blotting, Western; D002462:Cell Membrane / Q000201:enzymology; D005110:Extracellular Space / Q000201:enzymology; D005936:Glucans / Q000096:biosynthesis / Q000378:metabolism*; D005964:Glucosyltransferases / Q000235:genetics / Q000378:metabolism*; D009055:Mouth / Q000382:microbiology; D009154:Mutation; D010957:Plasmids; D013291:Streptococcus / Q000201:enzymology* / Q000235:genetics; D013295:Streptococcus mutans / Q000201:enzymology* / Q000235:genetics; D013298:Streptococcus sanguis / Q000378:metabolism; D014169:Transformation, Bacterial
D005936:Glucans; D005964:Glucosyltransferases