ArticleJournal of bacteriology1999
Topology of RbsC, a membrane component of the ribose transporter, belonging to the AraH superfamily.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Microbial membrane transport genes in maize rhizosphere under fertilization - a preliminary study.Scientific reports · 2026Article
- A plastid carbohydrate carrier mediates ribose recycling from nucleotide catabolism and glucose export from starch degradation.Nature communications · 2025Article
- RedB, a Member of the CRP/FNR Family, Functions as a Transcriptional Redox Brake.Microbiology spectrum · 2022Article
- High-throughput, signature-tagged mutagenic approach to identify novel virulence factors of Yersinia pestis CO92 in a mouse model of infection.Infection and immunity · 2015Article
- In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes.The Journal of biological chemistry · 2015Article
- Lack of genomic evidence of AI-2 receptors suggests a non-quorum sensing role for luxS in most bacteria.BMC microbiology · 2008Article
- Genome-wide transcriptional profiling of the Escherichia coli response to a proline-rich antimicrobial peptide.Antimicrobial agents and chemotherapy · 2004Article
- Topology of RbsC, the membrane component of the Escherichia coli ribose transporter.Journal of bacteriology · 2003Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RbsC of Escherichia coli is the hydrophobic membrane component of ribose uptake system classified as the ATP-binding cassette transporter. To understand the structure and function of RbsC, its transmembrane topology was investigated by using 64 RbsC-PhoA fusions isolated either specifically or randomly. In order to confirm the cytoplasmic location of the short C-terminal region (5 amino acids), inside-out or right-side-out membrane vesicles were generated, and the C-terminal region was found to be digested by carboxypeptidase A only in inside-out vesicles. This result is consistent with the model, based on the results of alkaline phosphatase fusions, in which the protein traverses the membrane six times and the N and C termini are exposed to the cytoplasm.
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