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PMID: 7171603 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Sucrose transport by Streptococcus mutans. Evidence for multiple transport systems.

Biochimica et biophysica acta ·Vol. 692 ·No. 3 ·1982-11-22 ·Pages 415-24

Slee AM, Tanzer JM

Abstract

The transport of sucrose by selected mutant and wild-type cells of Streptococcus mutans was studied using washed cocci harvested at appropriate phases of growth, incubated in the presence of fluoride and appropriately labelled substrates. The rapid sucrose uptake observed cannot be ascribed to possible extracellular formation of hexoses from sucrose and their subsequent transport, formation of intracellular glycogen-like polysaccharide, or binding of sucrose or extracellular glucans to the cocci. Rather, there are at least three discrete transport systems for sucrose, two of which are phosphoenolpyruvate-dependent phosphotransferases with relatively low apparent Km values and the other a non-phosphotransferase (non-PTS) third transport system (termed TTS) with a relatively high apparent Km. For strain 6715-13 mutant 33, the Km values are 6.25 X 10(-5) M, 2.4 X 10(-4) M, and 3.0 X 10(-3) M, respectively: strain NCTC-10449, the Km values are 7.1 X 10(-5) M, 2.5 X 10(-4) M and 3.3 X 10(-3) M, respectively. The two lower Km systems could not be demonstrated in mid-log phase glucose-adapted cocci, a condition known to repress sucrose-specific phosphotransferase activity, but under these conditions the highest Km system persists. Also, a mutant devoid of sucrose-specific phosphotransferase activity fails to evidence the two high affinity (low apparent Km) systems, but still has the lowest affinity (highest Km) system. There was essentially no uptake at 4 degrees C indicating these processes are energy dependent. The third transport system, whose nature is unknown, appears to function under conditions of sucrose abundance and rapid growth which are known to repress phosphoenolpyruvate-dependent sucrose-specific phosphotransferase activity in S. mutans. These multiple transport systems seem well-adapted to S. mutans which is faced with fluctuating supplies of sucrose in its natural habitat on the surfaces of teeth.

MeSH Terms
Biological Transport/drug effects Fluorides/pharmacology Glycoside Hydrolases/metabolism Hexosyltransferases/metabolism Kinetics Mutation Species Specificity Streptococcus mutans/metabolism Sucrose/metabolism beta-Fructofuranosidase
Chemicals
Sucrose Hexosyltransferases Glycoside Hydrolases beta-Fructofuranosidase Fluorides
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Slee A M
Tanzer J M
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1982-11-22
Pages
415-24
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
Grants
NIDCR NIH HHS · DE 03758 · United States
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