Mechanism of Folate Transport in Lactobacillus casei: Evidence for a Component Shared with the Thiamine and Biotin Transport Systems

@article{Henderson1979MechanismOF,
  title={Mechanism of Folate Transport in Lactobacillus casei: Evidence for a Component Shared with the Thiamine and Biotin Transport Systems},
  author={Gary B. Henderson and Edward M. Zevely and Frank M. Huennekens},
  journal={Journal of Bacteriology},
  year={1979},
  volume={137},
  pages={1308 - 1314}
}
Lactobacillus casei cells have been shown previously to utilize two separate binding proteins for the transport of folate and thiamine. Folate transport, however, was found to be strongly inhibited by thiamine in spite of the fact that the folate-binding protein has no measurable affinity for thiamine. This inhibition, which did not fluctuate with intracellular adenosine triphosphate levels, occurred only in cells containing functional transport systems for both vitamins and was noncompetitive… Expand
Irreversible inhibition of folate transport in Lactobacillus casei by covalent modification of the binding protein with carbodiimide-activated folate.
Abstract Activated folate formed by reaction of folic acid and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide irreversibly inhibits the folate transport system of Lactobacillus casei . CompleteExpand
Coupling of Energy to Folate Transport in Lactobacillus casei
TLDR
The results suggest that the active transport of folate into L. casei is energized by adenosine 5'-triphosphate or an equivalent energy-rich compound, and that coupling occurs not via the membrane-bound adenoine triphosphatase but by direct interaction of the energy source with a component of the transport system. Expand
Cation-Dependent Binding of Substrate to the Folate Transport Protein of Lactobacillus casei
TLDR
The results suggest that the folate transport protein of L. casei may contain both a substrate- and cation-binding site and that folate binds with a high affinity only after the cation -binding site has been occupied. Expand
Membrane-associated folate transport proteins.
TLDR
Bound [ 3 H]folate provides a convenient means for following the folate transport protein during purification and also for quantitating the yield and degree of purification achieved in each step. Expand
Kinetic evidence for two interconvertible forms of the folate transport protein from Lactobacillus casei
TLDR
F folate transport protein of L. casei exists in two forms which can be distinguished by the accessibility of the binding site to the external medium and whose amounts are dependent upon the presence of bound folate, the pH, and the energetic state of the cell. Expand
Differential interaction of cations with the thiamine and biotin transport proteins of Lactobacillus casei.
TLDR
Results suggest that the transport protein for the anionic vitamin, biotin, contains a binding site for cations, suggesting that protons can partially fulfill the cation requirement. Expand
On the transport mechanism of energy-coupling factor transporters
TLDR
The identification of an inhibitor of the ECF transporters from the organism Lactobacillus delbrueckii is described, which could be a first step in the development of a new type of antibiotics against pathogenic bacteria that rely on ECFtransporters for their vitamin uptake. Expand
Binding properties of the 5-methyltetrahydrofolate/methotrexate transport system in L1210 cells.
TLDR
The measured binding activity does not represent low-temperature transport of substrate into cells, since it is readily saturable with time and is eliminated by either washing the cells with buffer or by the addition of excess unlabeled substrate. Expand
Methotrexate-Resistant Subline of Lactobacillus caseit
A methotrexate-resistant subline of Lactobacillus casei has been isolated which transports folate at a reduced rate and contains a binding protein whose affinity for folate (Kd = 280 nM) isExpand
Functional and structural characterization of an ECF-type ABC transporter for vitamin B12
TLDR
A cobalamin-specific ECF-type ABC transporter from Lactobacillus delbrueckii is characterized and it is demonstrated that it mediates the specific, ATP-dependent uptake of cobalamina. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 24 REFERENCES
Binding and transport of thiamine by Lactobacillus casei
TLDR
Thiamine transport proceeds via a system whose general properties are typical of active uptake processes; entry of the vitamin into the cells requires energy, is temperature dependent, exhibits saturation kinetics, and is inhibited by substrate analogs. Expand
The folate and thiamine transport proteins of Lactobacillus casei.
TLDR
Two separate binding proteins, one specific for folate and the other for thiamine, have been isolated from membrane fragments of Lactobacillus casei and the ability of these compounds to inhibit the transport of the corresponding vitamins is paralleled by their ability to inhibit binding. Expand
Folate transport in Lactobacillus casei: solubilization and general properties of the binding protein.
TLDR
Evidence is presented to suggest that the binding protein functions as the carrier of folate during its transport into the cells. Expand
Evidence for binding protein-independent substrate translocation by the methylgalactoside transport system of Escherichia coli K12.
  • A. R. Robbins, B. Rotman
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1975
TLDR
It is reported here that only two genes, mgl A, B, and C, are required for active transport of substrate by the methylgalactose permease of E. coli K12; the galactose-binding protein is not required for substrate translocation. Expand
Different mechanisms of energy coupling for the active transport of proline and glutamine in Escherichia coli.
  • E. Berger
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1973
TLDR
The results suggest that proline transport is driven directly by an energy-rich membrane state, which can be generated by either electron transport or ATP hydrolysis, and Glutamine uptake, on the other hand, is apparently driven direct by phosphate-bond energy formed by way of oxidative or substrate-level phosphorylations. Expand
Purification and properties of a membrane-associated, folate-binding protein from Lactobacillus casei.
A folate-binding protein has been solubilized from Lactobacillus casei by treatment of membrane preparations with Triton X-100 in the presence of [3H]folate. The protein-folate complex was purifiedExpand
Sugar transport. II. Characterization of constitutive membrane-bound enzymes II of the Escherichia coli phosphotransferase system.
TLDR
It was shown that II-B, phosphatidylglycerol, and divalent cation interacted to give a sedimentable pellet which catalyzed the phosphorylation of the sugars in the presence of II-A and the phospho-HPr generating system. Expand
Energetics of galactose, proline, and glutamine transport in a cytochrome-deficient mutant of Salmonella typhimurium.
TLDR
Both osmotic shock-sensitive and -resistant systems were sensitive to uncouplers and to inhibitors of the membrane-bound Ca2+, Mg2+-activated adenosine triphosphatase, suggesting that uptake by both types of systems is energized in these cells by an electrochemical gradient of protons formed by ATP hydrolysis through the ATPase. Expand
Synthesis of Reserve Materials for Endogenous Metabolism in Streptococcus faecalis
TLDR
Endogenous metabolism cannot be detected by measurement of the adenosine triphosphate (ATP) pool in the organisms, but cells harvested after growth with excess energy source exhibit endogenous metabolism, which is correlated with a much higher concentration of ATP in the organism than occurs in the cells grown with limited energy source. Expand
Leucine binding protein and regulation of transport in E. coli.
TLDR
It was shown that the rapid exchange of external leucine for intracellular isoleucine via the LIV-I system could create an isoleUCine pseudoauxotrophy and account for the leucin sensitivity of E. coli. Expand
...
1
2
3
...