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Differential regulation of amidase- and formamidase-mediated ammonia production by the Helicobacter pylori fur repressor.

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Title: Differential regulation of amidase- and formamidase-mediated ammonia production by the Helicobacter pylori fur repressor.
Authors: Vliet, A.H.M. (Arnoud) van, Stoof, J. (Jeroen), Poppelaars, S.W. (Sophie), Bereswill, S. (Stefan), Homuth, G. (Georg), Kist, M. (Manfred), Kuipers, E.J. (Ernst), Kusters, J.G. (Johannes)
Source: Journal of Biological Chemistry vol. 278 no. 11, pp. 9052-9057
Publication Year: 2003
Collection: RePub - Publications from Erasmus University, Rotterdam
Subject Terms: Gene Expression Regulation, Amidohydrolases/*biosynthesis/metabolism, Ammonia/*metabolism, Bacterial Proteins/chemistry/*metabolism, Base Sequence, DNA/metabolism, Helicobacter pylori/*metabolism/pathogenicity, Humans, Iron-Regulatory Proteins/*metabolism, Iron/pharmacology, Models, Biological, Molecular Sequence Data, Nucleic Acid Hybridization, Plasmids/metabolism, Promoter Regions (Genetics), Protein Binding, RNA/metabolism, Repressor Proteins/chemistry/*metabolism, Research Support, Non-U.S. Gov't, Substrate Specificity, Transcription, Genetic, Urease/chemistry
Description: The production of high levels of ammonia allows the human gastric pathogen Helicobacter pylori to survive the acidic conditions in the human stomach. H. pylori produces ammonia through urease-mediated degradation of urea, but it is also able to convert a range of amide substrates into ammonia via its AmiE amidase and AmiF formamidase enzymes. Here data are provided that demonstrate that the iron-responsive regulatory protein Fur directly and indirectly regulates the activity of the two H. pylori amidases. In contrast to other amidase-positive bacteria, amidase and formamidase enzyme activities were not induced by medium supplementation with their respective substrates, acrylamide and formamide. AmiE protein expression and amidase enzyme activity were iron-repressed in H. pylori 26695 but constitutive in the isogenic fur mutant. This regulation was mediated at the transcriptional level via the binding of Fur to the amiE promoter region. In contrast, formamidase enzyme activity was not iron-repressed but was significantly higher in the fur mutant. This effect was not mediated at the transcriptional level, and Fur did not bind to the amiF promoter region. These roles of Fur in regulation of the H. pylori amidases suggest that the H. pylori Fur regulator may have acquired extra functions to compensate for the absence of other regulatory systems.
Document Type: article in journal/newspaper
File Description: application/pdf
Language: English
Relation: https://repub.eur.nl/pub/13127; urn:hdl:1765/13127
DOI: 10.1074/jbc.M207542200
Availability: https://repub.eur.nl/pub/13127
https://doi.org/10.1074/jbc.M207542200
Accession Number: edsbas.B3A856D3
Database: BASE
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  – Url: https://repub.eur.nl/pub/13127#
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  Data: Differential regulation of amidase- and formamidase-mediated ammonia production by the Helicobacter pylori fur repressor.
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  Data: <searchLink fieldCode="AR" term="%22Vliet%2C+A%2EH%2EM%2E+%28Arnoud%29+van%22">Vliet, A.H.M. (Arnoud) van</searchLink><br /><searchLink fieldCode="AR" term="%22Stoof%2C+J%2E+%28Jeroen%29%22">Stoof, J. (Jeroen)</searchLink><br /><searchLink fieldCode="AR" term="%22Poppelaars%2C+S%2EW%2E+%28Sophie%29%22">Poppelaars, S.W. (Sophie)</searchLink><br /><searchLink fieldCode="AR" term="%22Bereswill%2C+S%2E+%28Stefan%29%22">Bereswill, S. (Stefan)</searchLink><br /><searchLink fieldCode="AR" term="%22Homuth%2C+G%2E+%28Georg%29%22">Homuth, G. (Georg)</searchLink><br /><searchLink fieldCode="AR" term="%22Kist%2C+M%2E+%28Manfred%29%22">Kist, M. (Manfred)</searchLink><br /><searchLink fieldCode="AR" term="%22Kuipers%2C+E%2EJ%2E+%28Ernst%29%22">Kuipers, E.J. (Ernst)</searchLink><br /><searchLink fieldCode="AR" term="%22Kusters%2C+J%2EG%2E+%28Johannes%29%22">Kusters, J.G. (Johannes)</searchLink>
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  Data: Journal of Biological Chemistry vol. 278 no. 11, pp. 9052-9057
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  Data: 2003
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  Data: RePub - Publications from Erasmus University, Rotterdam
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  Data: <searchLink fieldCode="DE" term="%22Gene+Expression+Regulation%22">Gene Expression Regulation</searchLink><br /><searchLink fieldCode="DE" term="%22Amidohydrolases%2F*biosynthesis%2Fmetabolism%22">Amidohydrolases/*biosynthesis/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Ammonia%2F*metabolism%22">Ammonia/*metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Bacterial+Proteins%2Fchemistry%2F*metabolism%22">Bacterial Proteins/chemistry/*metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Base+Sequence%22">Base Sequence</searchLink><br /><searchLink fieldCode="DE" term="%22DNA%2Fmetabolism%22">DNA/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Helicobacter+pylori%2F*metabolism%2Fpathogenicity%22">Helicobacter pylori/*metabolism/pathogenicity</searchLink><br /><searchLink fieldCode="DE" term="%22Humans%22">Humans</searchLink><br /><searchLink fieldCode="DE" term="%22Iron-Regulatory+Proteins%2F*metabolism%22">Iron-Regulatory Proteins/*metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Iron%2Fpharmacology%22">Iron/pharmacology</searchLink><br /><searchLink fieldCode="DE" term="%22Models%22">Models</searchLink><br /><searchLink fieldCode="DE" term="%22Biological%22">Biological</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+Sequence+Data%22">Molecular Sequence Data</searchLink><br /><searchLink fieldCode="DE" term="%22Nucleic+Acid+Hybridization%22">Nucleic Acid Hybridization</searchLink><br /><searchLink fieldCode="DE" term="%22Plasmids%2Fmetabolism%22">Plasmids/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Promoter+Regions+%28Genetics%29%22">Promoter Regions (Genetics)</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+Binding%22">Protein Binding</searchLink><br /><searchLink fieldCode="DE" term="%22RNA%2Fmetabolism%22">RNA/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Repressor+Proteins%2Fchemistry%2F*metabolism%22">Repressor Proteins/chemistry/*metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Research+Support%22">Research Support</searchLink><br /><searchLink fieldCode="DE" term="%22Non-U%2ES%2E+Gov't%22">Non-U.S. Gov't</searchLink><br /><searchLink fieldCode="DE" term="%22Substrate+Specificity%22">Substrate Specificity</searchLink><br /><searchLink fieldCode="DE" term="%22Transcription%22">Transcription</searchLink><br /><searchLink fieldCode="DE" term="%22Genetic%22">Genetic</searchLink><br /><searchLink fieldCode="DE" term="%22Urease%2Fchemistry%22">Urease/chemistry</searchLink>
– Name: Abstract
  Label: Description
  Group: Ab
  Data: The production of high levels of ammonia allows the human gastric pathogen Helicobacter pylori to survive the acidic conditions in the human stomach. H. pylori produces ammonia through urease-mediated degradation of urea, but it is also able to convert a range of amide substrates into ammonia via its AmiE amidase and AmiF formamidase enzymes. Here data are provided that demonstrate that the iron-responsive regulatory protein Fur directly and indirectly regulates the activity of the two H. pylori amidases. In contrast to other amidase-positive bacteria, amidase and formamidase enzyme activities were not induced by medium supplementation with their respective substrates, acrylamide and formamide. AmiE protein expression and amidase enzyme activity were iron-repressed in H. pylori 26695 but constitutive in the isogenic fur mutant. This regulation was mediated at the transcriptional level via the binding of Fur to the amiE promoter region. In contrast, formamidase enzyme activity was not iron-repressed but was significantly higher in the fur mutant. This effect was not mediated at the transcriptional level, and Fur did not bind to the amiF promoter region. These roles of Fur in regulation of the H. pylori amidases suggest that the H. pylori Fur regulator may have acquired extra functions to compensate for the absence of other regulatory systems.
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  Data: https://repub.eur.nl/pub/13127; urn:hdl:1765/13127
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  Data: 10.1074/jbc.M207542200
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  Data: https://repub.eur.nl/pub/13127<br />https://doi.org/10.1074/jbc.M207542200
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  Data: edsbas.B3A856D3
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        Value: 10.1074/jbc.M207542200
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      – Text: English
    Subjects:
      – SubjectFull: Gene Expression Regulation
        Type: general
      – SubjectFull: Amidohydrolases/*biosynthesis/metabolism
        Type: general
      – SubjectFull: Ammonia/*metabolism
        Type: general
      – SubjectFull: Bacterial Proteins/chemistry/*metabolism
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      – SubjectFull: Base Sequence
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      – SubjectFull: Helicobacter pylori/*metabolism/pathogenicity
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      – SubjectFull: Iron-Regulatory Proteins/*metabolism
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      – SubjectFull: Plasmids/metabolism
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      – SubjectFull: RNA/metabolism
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      – TitleFull: Differential regulation of amidase- and formamidase-mediated ammonia production by the Helicobacter pylori fur repressor.
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            – TitleFull: Journal of Biological Chemistry vol. 278 no. 11, pp. 9052-9057
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