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HP1021 is a redox switch protein identified in Helicobacter pylori.

  • Szczepanowski, Piotr1
  • Noszka, Mateusz1
  • Żyła-Uklejewicz, Dorota1
  • Pikuła, Fabian1
  • Nowaczyk-Cieszewska, Malgorzata1
  • Krężel, Artur2
  • Stingl, Kerstin3
  • Zawilak-Pawlik, Anna1
  • 1 Department of Microbiology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław 53-114, Poland. , (Poland)
  • 2 Department of Chemical Biology, Faculty of Biotechnology, University of Wrocław, Wrocław 50-383, Poland. , (Poland)
  • 3 Department of Biological Safety, National Reference Laboratory for Campylobacter, German Federal Institute for Risk Assessment, Berlin 12277, Germany. , (Germany)
Published Article
Nucleic Acids Research
Oxford University Press
Publication Date
Jun 17, 2021
DOI: 10.1093/nar/gkab440
PMID: 34139017


Helicobacter pylori is a gram-negative, microaerophilic, pathogenic bacterium and a widespread colonizer of humans. H. pylori has developed mechanisms that enable it to overcome the harsh environment of the human stomach, including reactive oxygen species (ROS). Interestingly, up to now no typical regulator dedicated to the oxidative-stress response has been discovered. In this work, we reveal that the inhibitor of replication initiation HP1021 functions as a redox switch protein in H. pylori and plays an important role in response to oxidative stress of the gastric pathogen. Each of the two predicted HP1021 domains contains three cysteine residues. We show that the cysteine residues of HP1021 are sensitive to oxidation both in vitro and in vivo, and we demonstrate that HP1021 DNA-binding activity to oriC depends on the redox state of the protein. Moreover, Zn2+ modulates HP1021 affinity towards oriC template DNA. Transcription analysis of selected H. pylori genes by RT-qPCR indicated that HP1021 is directly involved in the oxygen-dependent control of H. pylori fecA3 and gluP genes, which are implicated in response to oxidative stress. In conclusion, HP1021 is a redox switch protein and could be a target for H. pylori control strategies. © The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

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