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

2.50
Hdl Handle:
http://hdl.handle.net/10547/293982
Title:
Solute-binding protein-dependent ABC transporters are responsible for solute efflux in addition to solute uptake
Authors:
Hosie, Arthur H.F. ( 0000-0002-1327-7901 ) ; Allaway, D.; Jones, Marion; Walshaw, D.L.; Johnston, A.W.B.; Poole, Philip S.
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.
Citation:
Hosie, A.H.F., Allaway, D., Jones, M.A., Walshaw, D.L. (2001) 'Solute-binding protein-dependent ABC transporters are responsible for solute efflux in addition to solute uptake', Molecular Microbiology, 40(6), pp.1449-1459
Publisher:
Wiley-Blackwell
Journal:
Molecular Microbiology
Issue Date:
2001
URI:
http://hdl.handle.net/10547/293982
DOI:
10.1046/j.1365-2958.2001.02497.x
Additional Links:
http://doi.wiley.com/10.1046/j.1365-2958.2001.02497.x
Type:
Article
Language:
en
ISSN:
0950-382X; 1365-2958
Appears in Collections:
Cell and Cryobiology Research Group

Full metadata record

DC FieldValue Language
dc.contributor.authorHosie, Arthur H.F.en_GB
dc.contributor.authorAllaway, D.en_GB
dc.contributor.authorJones, Marionen_GB
dc.contributor.authorWalshaw, D.L.en_GB
dc.contributor.authorJohnston, A.W.B.en_GB
dc.contributor.authorPoole, Philip S.en_GB
dc.date.accessioned2013-06-14T12:21:51Z-
dc.date.available2013-06-14T12:21:51Z-
dc.date.issued2001-
dc.identifier.citationHosie, A.H.F., Allaway, D., Jones, M.A., Walshaw, D.L. (2001) 'Solute-binding protein-dependent ABC transporters are responsible for solute efflux in addition to solute uptake', Molecular Microbiology, 40(6), pp.1449-1459en_GB
dc.identifier.issn0950-382X-
dc.identifier.issn1365-2958-
dc.identifier.doi10.1046/j.1365-2958.2001.02497.x-
dc.identifier.urihttp://hdl.handle.net/10547/293982-
dc.description.abstractThe 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.en_GB
dc.language.isoenen
dc.publisherWiley-Blackwellen_GB
dc.relation.urlhttp://doi.wiley.com/10.1046/j.1365-2958.2001.02497.xen_GB
dc.rightsArchived with thanks to Molecular Microbiologyen_GB
dc.subjectATP-binding cassetteen_GB
dc.subjectABC transporteren_GB
dc.subjectsolute movementen_GB
dc.titleSolute-binding protein-dependent ABC transporters are responsible for solute efflux in addition to solute uptakeen
dc.typeArticleen
dc.identifier.journalMolecular Microbiologyen_GB
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