uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • 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 diffusion properties of two atypical Dps from the cyanobacterium Nostoc punctiforme disclose interactions with ferredoxins and DNA
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics. Linköping Univ, Div Chem, Dept Phys Chem & Biol, Linköping, Sweden.
Aix Marseille Univ, CNRS, Inst Fresnel, Cent Marseille, Marseille, France; Inst Pasteur, Membrane Biochem & Transport, Paris, France.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics. Medicago AB, Uppsala, Sweden.
Show others and affiliations
2019 (English)In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1860, no 9, article id 148063Article in journal (Refereed) Published
Abstract [en]

Ferritin-like proteins, Dps (DNA-binding protein from starved cells), store iron and play a key role in the iron homeostasis in bacteria, yet their iron releasing machinery remains largely unexplored. The electron donor proteins that may interact with Dps and promote the mobilization of the stored iron have hitherto not been identified. Here, we investigate the binding capacity of the two atypical Dps proteins NpDps4 and NpDps5 from Nostoc punctiforme to isolated ferredoxins. We report NpDps-ferredoxin interactions by fluorescence correlation spectroscopy (FCS) and fluorescence resonance energy transfer (FRET) methods. Dynamic light scattering, size exclusion chromatography and native gel electrophoresis results show that NpDps4 forms a dodecamer at both pH 6.0 and pH 8.0, while NpDps5 forms a dodecamer only at pH 6.0. In addition, FCS data clearly reveal that the non-canonical NpDps5 interacts with DNA at pH 6.0. Our spectroscopic analysis shows that [FeS] centers of the three recombinantly expressed and isolated ferredoxins are properly incorporated and are consistent with their respective native states. The results support our hypothesis that ferredoxins could be involved in cellular iron homeostasis by interacting with Dps and assisting the release of stored iron.

Place, publisher, year, edition, pages
2019. Vol. 1860, no 9, article id 148063
Keywords [en]
Cyanobacteria, Ferredoxin, Ferritin-like proteins, Fluorescence correlation spectroscopy, FCS, Iron, Protein-protein interaction
National Category
Biochemistry and Molecular Biology Biophysics
Identifiers
URN: urn:nbn:se:uu:diva-395418DOI: 10.1016/j.bbabio.2019.148063ISI: 000486134900006PubMedID: 31419396OAI: oai:DiVA.org:uu-395418DiVA, id: diva2:1362986
Funder
Swedish Energy Agency, 11674-5EU, FP7, Seventh Framework Programme, 278242EU, Horizon 2020, 723241NordForsk, 82845Carl Tryggers foundation Available from: 2019-10-22 Created: 2019-10-22 Last updated: 2019-10-22Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMed

Authority records BETA

Moparthi, VamsiHowe, ChristophRaleiras, PatriciaStensjö, Karin

Search in DiVA

By author/editor
Moparthi, VamsiHowe, ChristophRaleiras, PatriciaStensjö, Karin
By organisation
Molecular Biomimetics
In the same journal
Biochimica et Biophysica Acta - Bioenergetics
Biochemistry and Molecular BiologyBiophysics

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 1 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • 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