Two closely related ABC transporters in streptococcus mutans are involved in disaccharide and/or oligosaccharide uptake.

2.50
Hdl Handle:
http://hdl.handle.net/10547/228322
Title:
Two closely related ABC transporters in streptococcus mutans are involved in disaccharide and/or oligosaccharide uptake.
Authors:
Webb, Alexander J.; Homer, Karen A.; Hosie, Arthur H.F. ( 0000-0002-1327-7901 )
Abstract:
Streptococcus mutans has a large number of transporters apparently involved in the uptake of carbohydrates. At least two of these, the multiple sugar metabolism transporter, MsmEFGK, and the previously uncharacterized MalXFGK, are members of the ATP-binding cassette (ABC) superfamily. Mutation analysis revealed that the MsmEFGK and MalXFGK transporters are principally involved in the uptake of distinct disaccharides and/or oligosaccharides. Furthermore, the data also indicated an unusual protein interaction between the components of these two related transporters. Strains lacking msmE (which encodes a solute binding protein) can no longer utilize raffinose or stachyose but grow normally on maltodextrins in the absence of MalT, a previously characterized EII(mal) phosphotransferase system component. In contrast, a mutant of malX (which encodes a solute binding protein) cannot utilize maltodextrins but grows normally on raffinose or stachyose. Radioactive uptake assays confirmed that MalX, but not MsmE, is required for uptake of [U-14C]maltotriose and that MalXFGK is principally involved in the uptake of maltodextrins with as many as 7 glucose units. Surprisingly, inactivation of the corresponding ATPase components did not result in an equivalent abolition of growth: the malK mutant can grow on maltotetraose as a sole carbon source, and the msmK mutant can utilize raffinose. We propose that the ATPase domains of these ABC transporters can interact with either their own or the alternative transporter complex. Such unexpected interaction of ATPase subunits with distinct membrane components to form complete multiple ABC transporters may be widespread in bacteria.
Affiliation:
Microbiology, King's College London Dental Institute, Floor 28, Guy's Tower, King's College London, Guy's Campus, London, SE1 9RT, United Kingdom.
Citation:
Two closely related ABC transporters in streptococcus mutans are involved in disaccharide and/or oligosaccharide uptake. 2008, 190 (1):168-78 J. Bacteriol.
Publisher:
American Society for Microbiology
Journal:
Journal of bacteriology
Issue Date:
Jan-2008
URI:
http://hdl.handle.net/10547/228322
DOI:
10.1128/JB.01509-07
PubMed ID:
17965163
Additional Links:
http://ukpmc.ac.uk/articles/PMC2223742
Type:
Article
Language:
en
ISSN:
1098-5530
Appears in Collections:
Cell and Cryobiology Research Group

Full metadata record

DC FieldValue Language
dc.contributor.authorWebb, Alexander J.en_GB
dc.contributor.authorHomer, Karen A.en_GB
dc.contributor.authorHosie, Arthur H.F.en_GB
dc.date.accessioned2012-06-11T10:53:39Z-
dc.date.available2012-06-11T10:53:39Z-
dc.date.issued2008-01-
dc.identifier.citationTwo closely related ABC transporters in streptococcus mutans are involved in disaccharide and/or oligosaccharide uptake. 2008, 190 (1):168-78 J. Bacteriol.en_GB
dc.identifier.issn1098-5530-
dc.identifier.pmid17965163-
dc.identifier.doi10.1128/JB.01509-07-
dc.identifier.urihttp://hdl.handle.net/10547/228322-
dc.description.abstractStreptococcus mutans has a large number of transporters apparently involved in the uptake of carbohydrates. At least two of these, the multiple sugar metabolism transporter, MsmEFGK, and the previously uncharacterized MalXFGK, are members of the ATP-binding cassette (ABC) superfamily. Mutation analysis revealed that the MsmEFGK and MalXFGK transporters are principally involved in the uptake of distinct disaccharides and/or oligosaccharides. Furthermore, the data also indicated an unusual protein interaction between the components of these two related transporters. Strains lacking msmE (which encodes a solute binding protein) can no longer utilize raffinose or stachyose but grow normally on maltodextrins in the absence of MalT, a previously characterized EII(mal) phosphotransferase system component. In contrast, a mutant of malX (which encodes a solute binding protein) cannot utilize maltodextrins but grows normally on raffinose or stachyose. Radioactive uptake assays confirmed that MalX, but not MsmE, is required for uptake of [U-14C]maltotriose and that MalXFGK is principally involved in the uptake of maltodextrins with as many as 7 glucose units. Surprisingly, inactivation of the corresponding ATPase components did not result in an equivalent abolition of growth: the malK mutant can grow on maltotetraose as a sole carbon source, and the msmK mutant can utilize raffinose. We propose that the ATPase domains of these ABC transporters can interact with either their own or the alternative transporter complex. Such unexpected interaction of ATPase subunits with distinct membrane components to form complete multiple ABC transporters may be widespread in bacteria.en_GB
dc.language.isoenen
dc.publisherAmerican Society for Microbiologyen_GB
dc.relation.urlhttp://ukpmc.ac.uk/articles/PMC2223742en_GB
dc.rightsArchived with thanks to Journal of bacteriologyen_GB
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subject.meshATP-Binding Cassette Transporters-
dc.subject.meshAmino Acid Sequence-
dc.subject.meshBiological Transport-
dc.subject.meshDNA Primers-
dc.subject.meshDisaccharides-
dc.subject.meshEscherichia coli-
dc.subject.meshKinetics-
dc.subject.meshMolecular Sequence Data-
dc.subject.meshMutation-
dc.subject.meshOligosaccharides-
dc.subject.meshPeptide Fragments-
dc.subject.meshPlasmids-
dc.subject.meshRecombinant Proteins-
dc.subject.meshStreptococcus mutans-
dc.titleTwo closely related ABC transporters in streptococcus mutans are involved in disaccharide and/or oligosaccharide uptake.en
dc.typeArticleen
dc.contributor.departmentMicrobiology, King's College London Dental Institute, Floor 28, Guy's Tower, King's College London, Guy's Campus, London, SE1 9RT, United Kingdom.en_GB
dc.identifier.journalJournal of bacteriologyen_GB
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