The sodium/proline transporter PutP of Helicobacter pylori.

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  • Additional Information
    • Source:
      Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
    • Publication Information:
      Original Publication: San Francisco, CA : Public Library of Science
    • Subject Terms:
      Amino Acid Transport Systems, Neutral/*genetics ; Amino Acid Transport Systems, Neutral/*metabolism ; Helicobacter pylori/*genetics ; Proline/*metabolism ; Sodium/*metabolism ; Symporters/*genetics; Amino Acid Transport Systems, Neutral/chemistry ; Binding Sites ; Biological Transport ; Escherichia coli Proteins/genetics ; Helicobacter pylori/metabolism ; Models, Molecular ; Sequence Homology ; Structure-Activity Relationship ; Symporters/chemistry ; Symporters/metabolism
    • Abstract:
      Helicobacter pylori is cause of chronic gastritis, duodenal ulcer and gastric carcinoma in humans. L-proline is a preferred energy source of the microaerophilic bacterium. Previous analyses revealed that HpputP and HpputA, the genes that are predicted to play a central role in proline metabolism as they encode for the proline transporter and proline dehydrogenase, respectively, are essential for stomach colonization. Here, the molecular basis of proline transport in H. pylori by HpPutP was investigated experimentally for the first time. Measuring radiolabeled substrate transport in H. pylori and E. coli heterologously expressing HpputP as well as in proteoliposomes reconstituted with HpPutP, we demonstrate that the observed proline transport in H. pylori is mediated by HpPutP. HpPutP is specific and exhibits a high affinity for L-proline. Notably, L-proline transport is exclusively dependent on Na(+) as coupling ion, i.e., Na(+)/L-proline symport, reminiscent to the properties of PutP of E. coli even though H. pylori lives in a more acidic environment. Homology model-based structural comparisons and substitution analyses identified amino acids crucial for function. HpPutP-catalyzed proline uptake was efficiently inhibited by the known proline analogs 3,4-dehydro-D,L-proline and L-azetidine-2-carboxylic acid.
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    • Accession Number:
      0 (Amino Acid Transport Systems, Neutral)
      0 (Escherichia coli Proteins)
      0 (Symporters)
      111565-48-1 (PutP protein, E coli)
      9DLQ4CIU6V (Proline)
      9NEZ333N27 (Sodium)
    • Publication Date:
      Date Created: 20131221 Date Completed: 20141021 Latest Revision: 20211021
    • Publication Date:
      20221213
    • Accession Number:
      PMC3866251
    • Accession Number:
      10.1371/journal.pone.0083576
    • Accession Number:
      24358297