Abstract
Strains of Salmonella typhimurium deficient in one or more of the proline transport systems have been constructed and used to study the mechanism of energy coupling to transport. Proline uptake through the major proline permease (PP-I, putP) is shown to be absolutely coupled to Na+ ions and not to H+ ions as has previously been assumed. Transport through the minor proline permease (PP-II, proP), however, is unaffected by the presence or absence of Na+. The effect of Na+ on the kinetics of proline uptake shows that external Na+ increases the Vmax for transport. It seems probable that proline transport through PP-I is also coupled to Na+ ions in Escherichia coli.
MeSH Terms
Amino Acid Transport Systems, Neutral
Biological Transport/drug effects
DNA Transposable Elements
Kinetics
Membrane Transport Proteins/genetics,metabolism
Potassium/pharmacology
Proline/metabolism
Salmonella typhimurium/enzymology,genetics
Sodium/metabolism
Species Specificity
Transduction, Genetic
Chemicals
Amino Acid Transport Systems, Neutral
DNA Transposable Elements
Membrane Transport Proteins
proline transporter
Proline
Sodium
Potassium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Cairney J
Higgins C F
Booth I R
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