The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor

Mendel, Ralf R.; Hercher, Thomas W.; Zupok, Arkadiusz; Hasnat, Muhammad Abrar; Leimkühler, Silke

doi:10.3390/inorganics8070043

Cited by 8 publications

(3 citation statements)

References 150 publications

(219 reference statements)

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“…On the other hand, heme utilization protein hut Z and heme carrier protein hut X had a higher accumulation for P. phosphoreum strains which are both part of an operon that binds heme and was suggested to act either as storage for said molecule or to facilitate its traffic from the membrane to proteins (Wyckoff et al, 2004 ). Finally, we found an increase of accumulation in iron-sulfur cluster assembly proteins for P. phosphoreum strains, namely, cofactors that are required for several essential pathways such as respiration, carbon metabolism, and protection from oxidizing agents (Mendel et al, 2020 ).…”

Section: Resultsmentioning

confidence: 95%

Impact of Modified Atmospheres on Growth and Metabolism of Meat-Spoilage Relevant Photobacterium spp. as Predicted by Comparative Proteomics

et al. 2022

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Modified atmosphere packaging (MAP) is a common strategy to selectively prevent the growth of certain species of meat spoiling bacteria. This study aimed to determine the impact of high oxygen MAP (70% O2, 30% CO2, red and white meats) and oxygen-free MAP (70% N2, 30% CO2, also white meat and seafood) on preventing the growth of spoiling photobacteria on meat. Growth of Photobacterium carnosum and P. phosphoreum was monitored in a meat simulation media under different gas mixtures of nitrogen, oxygen, and carbon dioxide, and samples were taken during exponential growth for a comparative proteomic analysis. Growth under air atmosphere appears optimal, particularly for P. carnosum. Enhanced protein accumulation affected energy metabolism, respiration, oxygen consuming reactions, and lipid usage. However, all the other atmospheres show some degree of growth reduction. An increase in oxygen concentration leads to an increase in enzymes counteracting oxidative stress for both species and enhancement of heme utilization and iron-sulfur cluster assembly proteins for P. phosphoreum. Absence of oxygen appears to switch the metabolism toward fermentative pathways where either ribose (P. phosphoreum) or glycogen (P. carnosum) appear to be the preferred substrates. Additionally, it promotes the use of alternative electron donors/acceptors, mainly formate and nitrate/nitrite. Stress response is manifested as an enhanced accumulation of enzymes that is able to produce ammonia (e.g., carbonic anhydrase, hydroxylamine reductase) and regulate osmotic stress. Our results suggest that photobacteria do not sense the environmental levels of carbon dioxide, but rather adapt to their own anaerobic metabolism. The regulation in presence of carbon dioxide is limited and strain-specific under anaerobic conditions. However, when oxygen at air-like concentration (21%) is present together with carbon dioxide (30%), the oxidative stress appears enhanced compared to air conditions (very low carbon dioxide), as explained if both gases have a synergistic effect. This is further supported by the increase in oxygen concentration in the presence of carbon dioxide. The atmosphere is able to fully inhibit P. carnosum, heavily reduce P. phosphoreum growth in vitro, and trigger diversification of energy production with higher energetic cost, highlighting the importance of concomitant bacteria for their growth on raw meat under said atmosphere.

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Section: Resultsmentioning

confidence: 95%

Impact of Modified Atmospheres on Growth and Metabolism of Meat-Spoilage Relevant Photobacterium spp. as Predicted by Comparative Proteomics

et al. 2022

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“…It also requires two reduced glutathione (GSH) molecules [ 41 ] ( Figure 4 ). What is interesting is that ISCU2 can donate a [2Fe–2S] cluster directly to the protein without the need of HSPA9/HSC20 [ 67 ] ( Figure 4 ). The export of newly assembled clusters requires three different compounds: one membrane channel protein ABCb7 (yeast protein atm1, ATP-binding cassette (ABC) transporter family) [ 45 ], one sulfhydryl oxidase (FAD-linked sulfhydryl oxidase (ALR) [ 68 ], and one reducing factor (glutathione) [ 20 ].…”

Section: Iron–sulfur Cluster Synthesismentioning

confidence: 99%

Sulfur Administration in Fe–S Cluster Homeostasis

2021

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Mitochondria are the key organelles of Fe–S cluster synthesis. They contain the enzyme cysteine desulfurase, a scaffold protein, iron and electron donors, and specific chaperons all required for the formation of Fe–S clusters. The newly formed cluster can be utilized by mitochondrial Fe–S protein synthesis or undergo further transformation. Mitochondrial Fe–S cluster biogenesis components are required in the cytosolic iron–sulfur cluster assembly machinery for cytosolic and nuclear cluster supplies. Clusters that are the key components of Fe–S proteins are vulnerable and prone to degradation whenever exposed to oxidative stress. However, once degraded, the Fe–S cluster can be resynthesized or repaired. It has been proposed that sulfurtransferases, rhodanese, and 3-mercaptopyruvate sulfurtransferase, responsible for sulfur transfer from donor to nucleophilic acceptor, are involved in the Fe–S cluster formation, maturation, or reconstitution. In the present paper, we attempt to sum up our knowledge on the involvement of sulfurtransferases not only in sulfur administration but also in the Fe–S cluster formation in mammals and yeasts, and on reconstitution-damaged cluster or restoration of enzyme’s attenuated activity.

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“…However, on the other hand, the depletion of Mo is lethal for most organisms [2]. Despite the Mo enzymes' ubiquitous presence in all kingdoms of life, there are exceptions, such as the common yeast Saccharomyces cerevisiae that survive without the possession of Mo enzymes [3].…”

Section: Introductionmentioning

confidence: 99%

Precise Quantification of Molybdate In Vitro by the FRET-Based Nanosensor ‘MolyProbe’

et al. 2022

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Molybdenum (Mo) is an essential trace element in all kingdoms of life. Mo is bioavailable as the oxyanion molybdate and gains biological activity in eukaryotes when bound to molybdopterin, forming the molybdenum cofactor. The imbalance of molybdate homeostasis results in growth deficiencies or toxic symptoms within plants, fungi and animals. Recently, fluorescence resonance energy transfer (FRET) methods have emerged, monitoring cellular and subcellular molybdate distribution dynamics using a genetically encoded molybdate-specific FRET nanosensor, named MolyProbe. Here, we show that the MolyProbe system is a fast and reliable in vitro assay for quantitative molybdate determination. We added a Strep-TagII affinity tag to the MolyProbe protein for quick and easy purification. This MolyProbe is highly stable, resistant to freezing and can be stored for several weeks at 4 °C. Furthermore, the molybdate sensitivity of the assay peaked at low nM levels. Additionally, The MolyProbe was applied in vitro for quantitative molybdate determination in cell extracts of the plant Arabidopsis thaliana, the fungus Neurospora crassa and the yeast Saccharomyces cerevisiae. Our results show the functionality of the Arabidopsis thaliana molybdate transporter MOT1.1 and indicate that FRET-based molybdate detection is an excellent tool for measuring bioavailable Mo.

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The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor

Cited by 8 publications

References 150 publications

Impact of Modified Atmospheres on Growth and Metabolism of Meat-Spoilage Relevant Photobacterium spp. as Predicted by Comparative Proteomics

Impact of Modified Atmospheres on Growth and Metabolism of Meat-Spoilage Relevant Photobacterium spp. as Predicted by Comparative Proteomics

Sulfur Administration in Fe–S Cluster Homeostasis

Precise Quantification of Molybdate In Vitro by the FRET-Based Nanosensor ‘MolyProbe’

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