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Solute-binding protein-dependent ABC transporters are responsible for solute efflux in addition to solute uptake

  • Arthur Hosie
    ,
  • D. Allaway
    ,
  • Marion Jones
    ,
  • D.L. Walshaw
    ,
  • A.W.B. Johnston
    ,
  • Philip S. Poole
  • University of Reading
Research Output:
Contribution to journal
Article
 Peer-review

Abstract

The ATP-binding cassette (ABC) transporter superfamily is one of the most widespread of all gene families and currently has in excess of 1100 members in organisms ranging from the Archaea to man. The movement of the diverse solutes of ABC transporters has been accepted as being strictly unidirectional, with recent models indicating that they are irreversible. However, contrary to this paradigm, we show that three solute-binding protein-dependent (SBP) ABC transporters of amino acids, i.e. the general amino acid permease (Aap) and the branched-chain amino acid permease (Bra) of Rhizobium leguminosarum and the histidine permease (His) of Salmonella typhimurium, are bidirectional, being responsible for efflux in addition to the uptake of solutes. The net solute movement measured for an ABC transporter depends on the rates of uptake and efflux, which are independent; a plateau is reached when both are saturated.

Publication Information

Output type

Research Output:
Contribution to journal
Article
 Peer-review

Original language

English

Pages from-to (Number of pages)

Pages 1449-1459

Journal (Volume, Issue Number)

Molecular Microbiology (Volume 40, Issue 6)

Publication milestones

  • Published - 01/01/2001

Publication status

Published - 01/01/2001

ISSN

0950-382X

Publication IDs

  • handle.net: 10547/293982
  • Scopus: 0034940069

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