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Appl. Environ. Microbiol., 05 1997, 1667-1673, Vol 63, No. 5
MM Vickerman and DB Clewell
The single glucosyltransferase (GTF) of Streptococcus gordonii Challis CH1
makes alpha 1,3- and alpha 1,6-linked glucans from sucrose. The GTF
carboxyl-terminal region has six direct repeats thought to be involved in
glucan binding. Strains with defined mutations in this region have been
described recently (M. M. Vickerman, M. C. Sulavik, P. E. Minick, and D. B.
Clewell, Infect. Immun. 64:5117-5128, 1996). Strain CH107 GTF has three
internal direct repeats deleted; the 59 carboxyl-terminal amino acids are
identical to those of the parental strain. This deletion resulted in
decreased enzyme activity but did not affect the amount of cell-associated
GTF protein. The GTFs of strains CH2RPE and CH4RPE have six and eight
direct repeats, respectively, but are both missing the 14 carboxyl-terminal
amino acids. Strain CH2RPE had significantly decreased levels of
cell-associated GTF; this decrease was not obviated by the increased number
of direct repeats in strain CH4RPE. Thus, the carboxyl-terminal amino acids
appeared to influence the amount of cell-associated GTF more than the
direct repeats. The qualitative and quantitative differences in the GTFs
did not affect the abilities of these strains to accumulate on
hydroxyapatite beads in the absence of sucrose. However, when sucrose was
added as a substrate for GTF, the mutant strains were unable to accumulate
on these surfaces to the same extent as the parent. These differences in
sucrose-associated accumulation may be due to changes in the nature of the
glucans produced by the different enzymes and/or cohesive interactions
between these glucans and the GTF on the surfaces of the growing
streptococci.
Copyright © 1997, American Society for Microbiology
Deletions in the carboxyl-terminal region of Streptococcus gordonii glucosyltransferase affect cell-associated enzyme activity and sucrose- associated accumulation of growing cells
Department of Microbiology and Immunology, School of Medicine, University of Michigan, Ann Arbor 48109, USA. vickerma@umich.edu
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