Fe–S proteins that regulate gene expression

Mettert, Erin L.; Kiley, Patricia J.

doi:10.1016/j.bbamcr.2014.11.018

Cited by 110 publications

(81 citation statements)

References 191 publications

(199 reference statements)

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“…Although the reaction constant for oxidation of the abundantly present cysteine residues is generally low, iron and iron clusters display much higher reactivity with H 2 O 2 , thus offering a limited number of candidates as exquisitely sensitive receptor modules (1,81,82). In support of such a possibility, multiple iron cluster-containing proteins induce transcriptional changes in bacteria, and thus might represent ancestral ROS-sensing signal transducers (83).…”

Section: Discussionmentioning

confidence: 99%

A respiratory chain controlled signal transduction cascade in the mitochondrial intermembrane space mediates hydrogen peroxide signaling

Patterson

Gerbeth

Thiru

et al. 2015

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

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Reactive oxygen species (ROS) such as hydrogen peroxide (H2O2) govern cellular homeostasis by inducing signaling. H2O2 modulates the activity of phosphatases and many other signaling molecules through oxidation of critical cysteine residues, which led to the notion that initiation of ROS signaling is broad and nonspecific, and thus fundamentally distinct from other signaling pathways. Here, we report that H2O2 signaling bears hallmarks of a regular signal transduction cascade. It is controlled by hierarchical signaling events resulting in a focused response as the results place the mitochondrial respiratory chain upstream of tyrosine-protein kinase Lyn, Lyn upstream of tyrosine-protein kinase SYK (Syk), and Syk upstream of numerous targets involved in signaling, transcription, translation, metabolism, and cell cycle regulation. The active mediators of H2O2 signaling colocalize as H2O2 induces mitochondria-associated Lyn and Syk phosphorylation, and a pool of Lyn and Syk reside in the mitochondrial intermembrane space. Finally, the same intermediaries control the signaling response in tissues and species responsive to H2O2 as the respiratory chain, Lyn, and Syk were similarly required for H2O2 signaling in mouse B cells, fibroblasts, and chicken DT40 B cells. Consistent with a broad role, the Syk pathway is coexpressed across tissues, is of early metazoan origin, and displays evidence of evolutionary constraint in the human. These results suggest that H2O2 signaling is under control of a signal transduction pathway that links the respiratory chain to the mitochondrial intermembrane space-localized, ubiquitous, and ancient Syk pathway in hematopoietic and nonhematopoietic cells.

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Section: Discussionmentioning

confidence: 99%

A respiratory chain controlled signal transduction cascade in the mitochondrial intermembrane space mediates hydrogen peroxide signaling

Patterson

Gerbeth

Thiru

et al. 2015

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

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“…The main regulators that mediate expression of NO detoxification systems and consequently N 2 O formation in S. Typhimurium and E. coli include NorR, NsrR and FNR (reviewed by Arkenberg, Runkel, Richardson, & Rowley, 2011;Mettert & Kiley, 2015;Spiro, 2007Spiro, , 2011Spiro, , 2012Tucker, Le Brun, Dixon, & Hutchings, 2010;Fig. 2B).…”

Section: Regulatory Proteinsmentioning

confidence: 99%

Nitrous Oxide Metabolism in Nitrate-Reducing Bacteria

Torres

Simon

Rowley

et al. 2016

Advances in Microbial Physiology

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Nitrous oxide (N2O) is an important greenhouse gas (GHG) with substantial global warming potential and also contributes to ozone depletion through photochemical nitric oxide (NO) production in the stratosphere. The negative effects of N2O on climate and stratospheric ozone make N2O mitigation an international challenge. More than 60% of global N2O emissions are emitted from agricultural soils mainly due to the application of synthetic nitrogen-containing fertilizers. Thus, mitigation strategies must be developed which increase (or at least do not negatively impact) on agricultural efficiency whilst decrease the levels of N2O released. This aim is particularly important in the context of the ever expanding population and subsequent increased burden on the food chain. More than two-thirds of N2O emissions from soils can be attributed to bacterial and fungal denitrification and nitrification processes. In ammonia-oxidizing bacteria, N2O is formed through the oxidation of hydroxylamine to nitrite. In denitrifiers, nitrate is reduced to N2 via nitrite, NO and N2O production. In addition to denitrification, respiratory nitrate ammonification (also termed dissimilatory nitrate reduction to ammonium) is another important nitrate-reducing mechanism in soil, responsible for the loss of nitrate and production of N2O from reduction of NO that is formed as a by-product of the reduction process. This review will synthesize our current understanding of the environmental, regulatory and biochemical control of N2O emissions by nitrate-reducing bacteria and point to new solutions for agricultural GHG mitigation.

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“…Each subunit carries a conventional [2Fe–2S] (2+;+) cluster that acts as a redox sensor, e.g., of oxidative stress. Only enteric bacteria, such as E. coli , carry the complete soxRS regulon; Ec SoxR directly activates global regulator Ec SoxS that controls transcription of over a hundred genes (cf [51, 52] and refs quoted therein). EPR studies on SoxR, described below, were typically aimed at relating FeS cluster redox state to physiological functioning, but we will focus here on evaluating the quality of their System-EPR approach.…”

Section: Case Study 3: Global Versus Specific Regulationmentioning

confidence: 99%

EPR spectroscopy of complex biological iron–sulfur systems

Hagen

2018

J Biol Inorg Chem

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From the very first discovery of biological iron–sulfur clusters with EPR, the spectroscopy has been used to study not only purified proteins but also complex systems such as respiratory complexes, membrane particles and, later, whole cells. In recent times, the emphasis of iron–sulfur biochemistry has moved from characterization of individual proteins to the systems biology of iron–sulfur biosynthesis, regulation, degradation, and implications for human health. Although this move would suggest a blossoming of System-EPR as a specific, non-invasive monitor of Fe/S (dys)homeostasis in whole cells, a review of the literature reveals limited success possibly due to technical difficulties in adherence to EPR spectroscopic and biochemical standards. In an attempt to boost application of System-EPR the required boundary conditions and their practical applications are explicitly and comprehensively formulated.

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Fe–S proteins that regulate gene expression

Cited by 110 publications

References 191 publications

A respiratory chain controlled signal transduction cascade in the mitochondrial intermembrane space mediates hydrogen peroxide signaling

A respiratory chain controlled signal transduction cascade in the mitochondrial intermembrane space mediates hydrogen peroxide signaling

Nitrous Oxide Metabolism in Nitrate-Reducing Bacteria

EPR spectroscopy of complex biological iron–sulfur systems

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