ArticleProceedings of the National Academy of Sciences of the United States of America1993
The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Domain interactions in the yeast ATP binding cassette transporter Ycf1p: intragenic suppressor analysis of mutations in the nucleotide binding domains.Journal of bacteriology · 2001Article
- The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil.Journal of bacteriology · 2000Article
- Expression and purification of the first nucleotide-binding domain and linker region of human multidrug resistance gene product: comparison of fusions to glutathione S-transferase, thioredoxin and maltose-binding protein.The Biochemical journal · 1999Article
- The SecA subunit of Escherichia coli preprotein translocase is exposed to the periplasm.Journal of bacteriology · 1998Article
- P-glycoprotein structure and evolutionary homologies.Cytotechnology · 1998Article
- In vitro disassembly and reassembly of an ABC transporter, the histidine permease.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation.Microbiology and molecular biology reviews : MMBR · 1998Review
- Frontiers in research on cystic fibrosis: understanding its molecular and chemical basis and relationship to the pathogenesis of the disease.Journal of bioenergetics and biomembranes · 1997Review
- Purification, characterization, and expression of CFTR nucleotide-binding domains.Journal of bioenergetics and biomembranes · 1997Article
- Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Characterization of membrane and protein interaction determinants of the Agrobacterium tumefaciens VirB11 ATPase.Journal of bacteriology · 1997Article
- Evidence that KpsT, the ATP-binding component of an ATP-binding cassette transporter, is exposed to the periplasm and associates with polymer during translocation of the polysialic acid capsule of Escherichia coli K1.Journal of bacteriology · 1997Article
- The VirB4 ATPase of Agrobacterium tumefaciens is a cytoplasmic membrane protein exposed at the periplasmic surface.Journal of bacteriology · 1997Article
- A phosphate transport system is required for symbiotic nitrogen fixation by Rhizobium meliloti.Journal of bacteriology · 1996Article
- The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane.Journal of bacteriology · 1995Article
- Interactions of VirB9, -10, and -11 with the membrane fraction of Agrobacterium tumefaciens: solubility studies provide evidence for tight associations.Journal of bacteriology · 1995Article
- In vivo reconstitution of an active siderophore transport system by a binding protein derivative lacking a signal sequence.Molecular & general genetics : MGG · 1995Article
- The Vibrio fischeri luminescence gene activator LuxR is a membrane-associated protein.Journal of bacteriology · 1993Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The membrane-bound complex of bacterial periplasmic permeases consists of two hydrophobic integral membrane proteins and two copies of a hydrophilic ATP-binding protein. The ATP-binding proteins from all periplasmic permeases display a high level of sequence similarity and are referred to as "conserved components." The conserved component from the histidine permease, HisP, has been postulated on the basis of genetic evidence to be accessible at the exterior membrane surface, in contrast to the commonly postulated association with the interior membrane surface as peripheral membrane proteins. We have used proteolysis and biotinylation of membrane vesicles to show that HisP is accessible to these reagents at the external surface and that this orientation depends on the presence of the two hydrophobic components, HisQ and HisM. Several binding-protein-independent hisP mutants are shown to produce HisP proteins that are more susceptible to proteases from the external membrane surface. Since the hydrophilic component is well conserved also in a group of eukaryotic transporters, which together with many prokaryotic systems form the superfamily of traffic ATPases, this insight about its membrane topology has general implications for understanding the molecular mechanism of action of this large superfamily, which includes the cystic fibrosis transmembrane conductance regulator and multidrug-resistance proteins.
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