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
The Dps4 from Nostoc punctiforme ATCC 29133 is a member of His-type FOC containing Dps protein class that can be broadly found among cyanobacteria
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Show others and affiliations
2019 (English)In: PLOS ONE, E-ISSN 1932-6203, Vol. 14, no 8, article id e0218300Article in journal (Refereed) Published
Abstract [en]

Dps proteins (DNA-binding proteins from starved cells) have been found to detoxify H2O2. At their catalytic centers, the ferroxidase center (FOC), Dps proteins utilize Fe2+ to reduce H2O2 and therefore play an essential role in the protection against oxidative stress and maintaining iron homeostasis. Whereas most bacteria accommodate one or two Dps, there are five different Dps proteins in Nostoc punctiforme, a phototrophic and filamentous cyanobacterium. This uncommonly high number of Dps proteins implies a sophisticated machinery for maintaining complex iron homeostasis and for protection against oxidative stress. Functional analyses and structural information on cyanobacterial Dps proteins are rare, but essential for understanding the function of each of the NpDps proteins. In this study, we present the crystal structure of NpDps4 in its metal-free, iron-and zinc-bound forms. The FOC coordinates either two iron atoms or one zinc atom. Spectroscopic analyses revealed that NpDps4 could oxidize Fe2+ utilizing O-2, but no evidence for its use of the oxidant H2O2 could be found. We identified Zn2+ to be an effective inhibitor of the O-2-mediated Fe2+ oxidation in NpDps4. NpDps4 exhibits a FOC that is very different from canonical Dps, but structurally similar to the atypical one from DpsA of Thermosynechococcus elongatus. Sequence comparisons among Dps protein homologs to NpDps4 within the cyanobacterial phylum led us to classify a novel FOC class: the His-type FOC. The features of this special FOC have not been identified in Dps proteins from other bacterial phyla and it might be unique to cyanobacterial Dps proteins.

Place, publisher, year, edition, pages
San Francisco: Public Library of Science , 2019. Vol. 14, no 8, article id e0218300
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-164427DOI: 10.1371/journal.pone.0218300ISI: 000484987900009PubMedID: 31369577Scopus ID: 2-s2.0-85070206372OAI: oai:DiVA.org:umu-164427DiVA, id: diva2:1363013
Available from: 2019-10-22 Created: 2019-10-22 Last updated: 2023-03-23Bibliographically approved

Open Access in DiVA

fulltext(3001 kB)236 downloads
File information
File name FULLTEXT01.pdfFile size 3001 kBChecksum SHA-512
e20842cdef6e637f325f3d7f9d49728451fe63387868eb34f3f94a81408bbdb11041e89fa52c12cfcb1be7b59534e8bc5cfe1bc8792e37b4e33fd3c8007b5f2a
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMedScopus

Authority records

Persson, Karina

Search in DiVA

By author/editor
Ho, Felix M.Persson, KarinaStensjo, Karin
By organisation
Department of Chemistry
In the same journal
PLOS ONE
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar
Total: 236 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 387 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