Umeå University's logo

umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).ORCID iD: 0000-0003-0864-9798
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).
Show others and affiliations
2016 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 113, no 51, p. 14733-14738Article in journal (Refereed) Published
Abstract [en]

Infection by the human bacterial pathogen Listeria monocytogenes is mainly controlled by the positive regulatory factor A (PrfA), a member of the Crp/Fnr family of transcriptional activators. Published data suggest that PrfA requires the binding of a cofactor for full activity, and it was recently proposed that glutathione (GSH) could fulfill this function. Here we report the crystal structures of PrfA in complex with GSH and in complex with GSH and its cognate DNA, the hly operator PrfA box motif. These structures reveal the structural basis for a GSH-mediated allosteric mode of activation of PrfA in the cytosol of the host cell. The crystal structure of PrfAWT in complex only with DNA confirms that PrfAWT can adopt a DNA binding-compatible structure without binding the GSH activator molecule. By binding to PrfA in the cytosol of the host cell, GSH induces the correct fold of the HTH motifs, thus priming the PrfA protein for DNA interaction.

Place, publisher, year, edition, pages
2016. Vol. 113, no 51, p. 14733-14738
Keywords [en]
Listeria, PrfA, activation, glutathione, virulence
National Category
Organic Chemistry Medical Genetics
Identifiers
URN: urn:nbn:se:umu:diva-128915DOI: 10.1073/pnas.1614028114ISI: 000390044900062Scopus ID: 2-s2.0-85006434755OAI: oai:DiVA.org:umu-128915DiVA, id: diva2:1057771
Available from: 2016-12-19 Created: 2016-12-19 Last updated: 2023-03-24Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textScopus

Authority records

Hall, MichaelGrundström, ChristinBegum, AfshanLindberg, Mikael J.Sauer, Uwe H.Almqvist, FredrikJohansson, JörgenSauer-Eriksson, A. Elisabeth

Search in DiVA

By author/editor
Hall, MichaelGrundström, ChristinBegum, AfshanLindberg, Mikael J.Sauer, Uwe H.Almqvist, FredrikJohansson, JörgenSauer-Eriksson, A. Elisabeth
By organisation
Department of ChemistryUmeå Centre for Microbial Research (UCMR)Department of Molecular Biology (Faculty of Medicine)Molecular Infection Medicine Sweden (MIMS)
In the same journal
Proceedings of the National Academy of Sciences of the United States of America
Organic ChemistryMedical Genetics

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 896 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf