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The two Dps proteins, NpDps2 and NpDps5, are involved in light-induced oxidative stress tolerance in the N-2-fixing cyanobacterium Nostoc punctiforme
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Department of Chemistry – Ångström Laboratory, Uppsala University, Uppsala, Sweden.
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2016 (English)In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1857, no 11, 1766-1776 p.Article in journal (Refereed) Published
Abstract [en]

Cyanobacteria are photosynthetic prokaryotes that are considered biotechnologically prominent organisms for production of high-value compounds. Cyanobacteria are subject to high-light intensities, which is a challenge that needs to be addressed in design of efficient bio-engineered photosynthetic organisms. Dps proteins are members of the ferritin superfamily and are omnipresent in prokaryotes. They play a major role in oxidative stress protection and iron homeostasis. The filamentous, heterocyst-forming Nostoc punctiforme, has five Dps proteins. In this study we elucidated the role of these Dps proteins in acclimation to high light intensity, the gene loci organization and the transcriptional regulation of all five dps genes in N. punctiforme was revealed, and dps-deletion mutant strains were used in physiological characterization. Two mutants defective in Dps2 and Dps5 activity displayed a reduced fitness under increased illumination, as well as a differential Photosystem (PS) stoichiometry, with an elevated Photosystem II to Photosystem I ratio in the dps5 deletion strain. This work establishes a Dps-mediated link between light tolerance, H2O2 detoxification, and iron homeostasis, and provides further evidence on the non-redundant role of multiple Dps proteins in this multicellular cyanobacterium.

Place, publisher, year, edition, pages
Elsevier, 2016. Vol. 1857, no 11, 1766-1776 p.
Keyword [en]
adaptation, cyanobacteria, ferritin, photosystem, light-stress, ROS
National Category
Biochemistry and Molecular Biology Biophysics
Identifiers
URN: urn:nbn:se:umu:diva-127229DOI: 10.1016/j.bbabio.2016.08.003ISI: 000384867400006OAI: oai:DiVA.org:umu-127229DiVA: diva2:1046748
Available from: 2016-11-15 Created: 2016-11-03 Last updated: 2016-11-15Bibliographically approved

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Dzhygyr, Ievgen
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Department of Molecular Biology (Faculty of Medicine)
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