Biosynthesis of selenate reductase in Salmonella enterica: critical roles for the signal peptide and DmsD

Connelly, Katherine R. S.; Stevenson, Calum; Kneuper, Holger; Sargent, Frank

doi:10.1099/mic.0.000381

Cited by 9 publications

(4 citation statements)

References 44 publications

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“…This NarG or NarZ nitrate reductase dependent reduction was later confirmed in other bacteria (Sabaty et al, 2001), with shared mechanisms and thus demonstrating cross-reactivities between microbial selenate and nitrate enzymatic reduction (Watts et al, 2005). Another CISM enzyme encoded by the ynfEFGH operon in Salmonella enterica was also shown to be responsible for the respiration of selenate to selenite, and subsequently converting the latter to SeNMs (Connelly et al, 2016). A cartoon description of a CISM enzyme process is shown in Figure 10.4.…”

Section: Proteins Involved In Selenium Nanoparticle Synthesismentioning

confidence: 81%

Se nanoparticle manufacturing for medical applications

Presentato¹,

Piacenza²,

Turner³

2021

Environmental Technologies to Treat Selenium Pollution

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The use of biological material or various life forms to produce nanomaterials is routed in the idea that their use will be more eco-friendly than chemically synthesized materials. The present chapter focuses on the current knowledge of how biological organisms and their associated biomolecules or biomass reduce selenium (Se) oxyanions to Se 0 atoms (Figure 10.1). The Se atoms then subsequently assemble on the nanoscale, thus producing 'biogenic' Se nanoparticles (BioSeNPs).The world of 'very small materials' implies the manipulation of matter at the molecular or atomic level (Horikoshi & Serpone, 2013), a field known as nanotechnology. Materials scaled down to the nano range (1-100 nm) are defined as nanomaterials (NMs), and possess unique physical-chemical properties arising from their high surface-to-volume ratio, large surface energy, and high spatial confinement (Cao, 2004;Yuwen & Wang, 2013). NMs exist in various sizes and shapes including nanoparticles (NPs), nanorods (NRs), quantum dots (QDs), nanowires (NWs), and nanotubes (NTs) (Rao et al., 2004). These materials have enhanced chemical, catalytic, mechanical, electrical and opto-magnetic properties (Appenzeller, 1991;Yuwen & Wang, 2013). Hence, NMs can be applied in a vast range of applications such as: biomedicine and biotechnologies, energy production, food and chemical industries, environmental engineering, mechanics,

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Section: Proteins Involved In Selenium Nanoparticle Synthesismentioning

confidence: 81%

Se nanoparticle manufacturing for medical applications

Presentato¹,

Piacenza²,

Turner³

2021

Environmental Technologies to Treat Selenium Pollution

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“…Interestingly, some complex Tat substrates have signal peptides that contain greatly extended n-regions prior to the twin-arginine motif (39). Such extensions are almost invariably found on substrates that bind redox cofactors and/or partner proteins prior to export, and they appear to serve as binding sites for dedicated chaperones that co-ordinate folding and assembly (40)(41)(42)(43)(44). FecR is distinct from these Tat substrates since it does not contain any redox cofactor, and its signal sequence n-region is considerably longer than other Tat signal peptide n-regions.…”

Section: Discussionmentioning

confidence: 99%

Ferric Citrate Regulator FecR Is Translocated across the Bacterial Inner Membrane via a Unique Twin-Arginine Transport-Dependent Mechanism

et al. 2020

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In Escherichia coli, citrate-mediated iron transport is a key nonheme pathway for the acquisition of iron. Binding of ferric citrate to the outer membrane protein FecA induces a signal cascade that ultimately activates the cytoplasmic sigma factor FecI, resulting in transcription of the fecABCDE ferric citrate transport genes. Central to this process is signal transduction mediated by the inner membrane protein FecR. FecR spans the inner membrane through a single transmembrane helix, which is flanked by cytoplasm- and periplasm-orientated moieties at the N and C termini. The transmembrane helix of FecR resembles a twin-arginine signal sequence, and the substitution of the paired arginine residues of the consensus motif decouples the FecR-FecI signal cascade, rendering the cells unable to activate transcription of the fec operon when grown on ferric citrate. Furthermore, the fusion of beta-lactamase C-terminal to the FecR transmembrane helix results in translocation of the C-terminal domain that is dependent on the twin-arginine translocation (Tat) system. Our findings demonstrate that FecR belongs to a select group of bitopic inner membrane proteins that contain an internal twin-arginine signal sequence. IMPORTANCE Iron is essential for nearly all living organisms due to its role in metabolic processes and as a cofactor for many enzymes. The FecRI signal transduction pathway regulates citrate-mediated iron import in many Gram-negative bacteria, including Escherichia coli. The interactions of FecR with the outer membrane protein FecA and cytoplasmic anti-sigma factor FecI have been extensively studied. However, the mechanism by which FecR inserts into the membrane has not previously been reported. In this study, we demonstrate that the targeting of FecR to the cytoplasmic membrane is dependent on the Tat system. As such, FecR represents a new class of bitopic Tat-dependent membrane proteins with an internal twin-arginine signal sequence.

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“…An FNR binding site was found upstream of the ynfE gene, suggesting that SeO 4 2− reduction in this bacterium occurred in anaerobic conditions. ynfE gene is located in the ynfEGHdmsD operon [234], and a high structural identity is observed between the selenate reductase of this bacterium and selenate reductases found in Gammaproteobacteria [235]. FNR is a general regulator system for fumarate and nitrate reductases and well regulates all CISMS (complex iron sulfur-molybdo enzymes).…”

Section: Seleniummentioning

confidence: 96%

Use of Microbial Consortia in Bioremediation of Metalloid Polluted Environments

et al. 2023

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Metalloids are released into the environment due to the erosion of the rocks or anthropogenic activities, causing problems for human health in different world regions. Meanwhile, microorganisms with different mechanisms to tolerate and detoxify metalloid contaminants have an essential role in reducing risks. In this review, we first define metalloids and bioremediation methods and examine the ecology and biodiversity of microorganisms in areas contaminated with these metalloids. Then we studied the genes and proteins involved in the tolerance, transport, uptake, and reduction of these metalloids. Most of these studies focused on a single metalloid and co-contamination of multiple pollutants were poorly discussed in the literature. Furthermore, microbial communication within consortia was rarely explored. Finally, we summarized the microbial relationships between microorganisms in consortia and biofilms to remove one or more contaminants. Therefore, this review article contains valuable information about microbial consortia and their mechanisms in the bioremediation of metalloids.

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Biosynthesis of selenate reductase in Salmonella enterica: critical roles for the signal peptide and DmsD

Cited by 9 publications

References 44 publications

Se nanoparticle manufacturing for medical applications

Se nanoparticle manufacturing for medical applications

Ferric Citrate Regulator FecR Is Translocated across the Bacterial Inner Membrane via a Unique Twin-Arginine Transport-Dependent Mechanism

Use of Microbial Consortia in Bioremediation of Metalloid Polluted Environments

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