Cellular and functional specificity among ferritin‐like proteins in the multicellular cyanobacterium <i><scp>N</scp>ostoc punctiforme</i>

Ekman, Martin; Sandh, Gustaf; Nenninger, Anja; Oliveira, Paulo; Stensjö, Karin

doi:10.1111/1462-2920.12233

Cited by 27 publications

(66 citation statements)

References 73 publications

(112 reference statements)

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“…Two clusters encoding respiratory terminal oxidases, cox2 and cox3, were found to be expressed specifically in heterocysts and shown to be essential for diazotrophic growth in Anabaena (14,15). Additionally, several other systems of protection against O 2 and ROS were recently found to be required to maintain the activity of nitrogenase or diazotrophic growth, emphasizing the ultimate importance of microoxic conditions for proper functioning of the N 2 -fixing machinery (16)(17)(18)(19).…”

Section: Significancementioning

confidence: 99%

Heterocyst-specific flavodiiron protein Flv3B enables oxic diazotrophic growth of the filamentous cyanobacterium Anabaena sp. PCC 7120

Ermakova

Battchikova

Richaud

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Flavodiiron proteins are known to have crucial and specific roles in photoprotection of photosystems I and II in cyanobacteria. The filamentous, heterocyst-forming cyanobacterium Anabaena sp. strain PCC 7120 contains, besides the four flavodiiron proteins Flv1A, Flv2, Flv3A, and Flv4 present in vegetative cells, two heterocyst-specific flavodiiron proteins, Flv1B and Flv3B. Here, we demonstrate that Flv3B is responsible for light-induced O 2 uptake in heterocysts, and that the absence of the Flv3B protein severely compromises the growth of filaments in oxic, but not in microoxic, conditions. It is further demonstrated that Flv3B-mediated photosynthetic O 2 uptake has a distinct role in heterocysts which cannot be substituted by respiratory O 2 uptake in the protection of nitrogenase from oxidative damage and, thus, in an efficient provision of nitrogen to filaments. In line with this conclusion, the Δflv3B strain has reduced amounts of nitrogenase NifHDK subunits and shows multiple symptoms of nitrogen deficiency in the filaments. The apparent imbalance of cytosolic redox state in Δflv3B heterocysts also has a pronounced influence on the amounts of different transcripts and proteins. Therefore, an O 2 -related mechanism for control of gene expression is suggested to take place in heterocysts.nitrogen fixation | oxygen protection | photosynthesis

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Section: Significancementioning

confidence: 99%

Heterocyst-specific flavodiiron protein Flv3B enables oxic diazotrophic growth of the filamentous cyanobacterium Anabaena sp. PCC 7120

Ermakova

Battchikova

Richaud

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…presents numerous similarities as other organisms (Liang et al, 2012;Liang et al, 2013;Oren et al, 2019;Wang et al, 2019). In general, the dehydration signal leads to stimulation of the defence system, following by vast accumulation of stressresponsive proteins, including APX, GPX, SOD and DNA-binding proteins to prevent or reverse reactive oxygen species (ROS) damage (Ekman et al, 2014). In addition, species-specific metabolic pathways involved in stress tolerance were reprogrammed to generate compatible metabolites such as trehalose and antioxidants like ascorbate, glutathione and vitamins (Dinakar and Bartels, 2013;Morano, 2014).…”

Section: Introductionmentioning

confidence: 99%

Dynamic expression of intra‐ and extra‐cellular proteome and the influence of epiphytic bacteria for Nostoc flagelliforme in response to rehydration

Wang

Yang

et al. 2020

Environmental Microbiology

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Summary Nostoc flagelliforme is well known for its strong ecological adaptability in inhabiting desert biological soil crusts. However, the mechanism of its recovery from quiescent to active state after prolonged dormancy remains poorly characterized. Especially how exoproteome be related to the adaptive strategies and participate in the microalgae‐bacteria interaction. In the present work, we analysed the intra‐ and extra‐cellular proteome of N. flagelliforme over a complete rehydration period both in sterilization and in natural condition for the first time. The protein expression profile for N. flagelliforme has more fluctuations during the first 1 h after wetting but been relatively steady after fully hydrated. According to the extracellular proteomic datasets, we found a dynamic secretion of various extracellular hydrolytic enzymes and membrane transport proteins, which were related to peptidoglycan digestion and nutrient exchange respectively. Two‐hundred and thirteen differentially expressed proteins induced by sterilization also reflect variation in nutrient exchange and highlight symbiosis between N. flagelliforme and surrounding bacteria. We also identified 112 phosphopeptides and 217 phosphorylation site of 95 protein of hydrated N. flagelliforme. The time course datasets we present here will be a reference for understanding the molecular processes underlying N. flagelliforme resuscitation and its potential role in microbial community diversification and soil desertification control.

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“…In cyanobacteria the existence of multiple Dps proteins has been found to be rather common [13,14]. But most of the more well-studied Dps proteins originate from pathogens that possess only one or two Dps proteins [2,15–17].…”

Section: Introductionmentioning

confidence: 99%

“…To learn specifically more about cyanobacterial Dps proteins, we have collected data on the different NpDps from N. punctiforme in the past years to identify their physiological roles. In an earlier study [13] we hypothesized that, despite all belonging to the Dps protein family, they might differ in their biochemical properties and thus in their physiological function.…”

Section: Introductionmentioning

confidence: 99%

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The Dps4 fromNostoc punctiformeATCC 29133 is a member of His-type FOC containing Dps protein class that can be broadly found among cyanobacteria

Howe

Moparthi

et al. 2019

Preprint

Self Cite

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25Dps proteins (DNA-binding proteins from starved cells) have been found to detoxify H 2 O 2 . At 26 their catalytic centers, the ferroxidase center (FOC), Dps proteins utilize Fe 2+ to reduce H 2 O 2 27 and therefore play an essential role in the protection against oxidative stress and maintaining 28 iron homeostasis. Whereas most bacteria accommodate one or two Dps, there are five 29 different Dps proteins in Nostoc punctiforme, a phototrophic and filamentous cyanobacterium. 30 This uncommonly high number of Dps proteins implies a sophisticated machinery for 31 maintaining complex iron homeostasis and for protection against oxidative stress. Functional 32 analyses and structural information on cyanobacterial Dps proteins are rare, but essential for 33 understanding the function of each of the NpDps proteins. In this study, we present the crystal 34 structure of NpDps4 in its metal-free, iron-and zinc-bound forms. The FOC coordinates either 35 two iron atoms or one zinc atom. Spectroscopic analyses revealed that NpDps4 could oxidize 36 Fe 2+ utilizing O 2 , but no evidence for its use of the oxidant H 2 O 2 could be found. We identified 37 Zn 2+ to be an effective inhibitor of the O 2 -mediated Fe 2+ oxidation in NpDps4. NpDps4 exhibits 38 a FOC that is very different from canonical Dps, but structurally similar to the atypical one from 39 DpsA of Thermosynechococcus elongatus. Sequence comparisons among Dps protein 40 homologs to NpDps4 within the cyanobacterial phylum led us to classify a novel FOC class: 41 the His-type FOC. The features of this special FOC have not been identified in Dps proteins 42 from other bacterial phyla and it might be unique to cyanobacterial Dps proteins.43 Keywords: ferroxidase center, iron, oxidative stress, crystal structure, reactive oxygen 44 species 45 46 3 49 bacterioferritins (bfr) and ferritins (ftn). Dps proteins exhibit a remarkable three-dimensional 50 structure consisting of twelve monomers (or six dimers), forming a spherically shaped protein 51 complex with a hollow spherical interior [2,3]. 52 On the inside, each dimeric interface creates two identical catalytic centers, called the 53 ferroxidase centers (FOC). There, the oxidation of ferrous iron (Fe 2+ ) to ferric (Fe 3+ ) takes 54 place and an iron oxide mineral core consisting of up to 500 Fe atoms can be formed [4]. 55 Canonical FOCs in Dps proteins consist of five conserved amino acids, namely two His and 56 one Asp from one monomer as well as one Glu and one Asp from the adjacent monomer at 57 the dimer interface.58To reach the catalytic center, the Fe 2+ ions have been suggested to travel through two types 59 of pores that are connecting the internal cavity with the exterior [2]. One pore type is the ferritin-60 like pore, which is named after their structural similarity to the iron entrance pores in ferritins. 61The ferritin-like pore has been frequently assigned to be the iron entrance pore due to its 62 negatively charged character in canonical Dps structures. The other pore type, the Dps-type 63 pore, i...

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Cellular and functional specificity among ferritin‐like proteins in the multicellular cyanobacterium Nostoc punctiforme

Cited by 27 publications

References 73 publications

Heterocyst-specific flavodiiron protein Flv3B enables oxic diazotrophic growth of the filamentous cyanobacterium Anabaena sp. PCC 7120

Heterocyst-specific flavodiiron protein Flv3B enables oxic diazotrophic growth of the filamentous cyanobacterium Anabaena sp. PCC 7120

Dynamic expression of intra‐ and extra‐cellular proteome and the influence of epiphytic bacteria for Nostoc flagelliforme in response to rehydration

The Dps4 fromNostoc punctiformeATCC 29133 is a member of His-type FOC containing Dps protein class that can be broadly found among cyanobacteria

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