Common themes and variations in the rhodanese superfamily

Cipollone, Rita; Ascenzi, Paolo; Visca, Paolo

doi:10.1080/15216540701206859

Cited by 210 publications

(226 citation statements)

References 52 publications

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“…Indeed, characterizing rhodanese physiological function in an organism is a challenge due to the abundance of potential rhodanese/rhodanese-like proteins within the same genome. As an example, E. coli and Pseudomonas aeruginosa have, respectively, 9 and 10 annotated rhodaneses or rhodanese-like proteins in their genome (18,35). This redundancy supports the notion that rhodaneses are involved in distinct cellular processes.…”

Section: Discussionmentioning

confidence: 56%

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Rhodanese Functions as Sulfur Supplier for Key Enzymes in Sulfur Energy Metabolism

Aussignargues¹,

Giuliani²,

Infossi

et al. 2012

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 56%

“…They catalyze in vitro the transfer of a sulfur atom from thiosulfate (sulfur donor) to cyanide (sulfur acceptor) (18,19). Rhodanese-like proteins share a common characteristic "rhodanese-fold" and catalyze a similar reaction using other sulfur donors (like polysulfide for Sud) to transfer sulfur to nucleophilic sulfur acceptors.…”

mentioning

confidence: 99%

Rhodanese Functions as Sulfur Supplier for Key Enzymes in Sulfur Energy Metabolism

Aussignargues¹,

Giuliani²,

Infossi

et al. 2012

Journal of Biological Chemistry

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“…These results reveal that 45% of all sulfide-responsive genes in the R. capsulatus genome are directly or indirectly regulated by SqrR. The identified sulfideresponsive genes include a number of genes known to function in sulfur metabolism or assimilation, including thiosulfate-sulfite oxidoreductases and thiosulfate sulfurtransferases or rhodanese homology domain proteins (33,34), whose expression is strongly repressed by SqrR. Although originally described as functioning in cyanide detoxification (35), sulfurtransferases and structurally unrelated single-Cys-containing TusA domains (36) are generally involved in persulfide shuttling, and are capable of accepting sulfur from a variety of RSS, including thiosulfate and lowmolecular-weight persulfides (37).…”

Section: Resultsmentioning

confidence: 96%

Sulfide-responsive transcriptional repressor SqrR functions as a master regulator of sulfide-dependent photosynthesis

Shimizu

Shen

Fang

et al. 2017

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

113

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Sulfide was used as an electron donor early in the evolution of photosynthesis, with many extant photosynthetic bacteria still capable of using sulfur compounds such as hydrogen sulfide (H 2 S) as a photosynthetic electron donor. Although enzymes involved in H 2 S oxidation have been characterized, mechanisms of regulation of sulfide-dependent photosynthesis have not been elucidated. In this study, we have identified a sulfide-responsive transcriptional repressor, SqrR, that functions as a master regulator of sulfide-dependent gene expression in the purple photosynthetic bacterium Rhodobacter capsulatus. SqrR has three cysteine residues, two of which, C41 and C107, are conserved in SqrR homologs from other bacteria. Analysis with liquid chromatography coupled with an electrospray-interface tandem-mass spectrometer reveals that SqrR forms an intramolecular tetrasulfide bond between C41 and C107 when incubated with the sulfur donor glutathione persulfide. SqrR is oxidized in sulfidestressed cells, and tetrasulfide-cross-linked SqrR binds more weakly to a target promoter relative to unmodified SqrR. C41S and C107S R. capsulatus SqrRs lack the ability to respond to sulfide, and constitutively repress target gene expression in cells. These results establish that SqrR is a sensor of H 2 S-derived reactive sulfur species that maintain sulfide homeostasis in this photosynthetic bacterium and reveal the mechanism of sulfide-dependent transcriptional derepression of genes involved in sulfide metabolism.sulfide sensor | photosynthesis regulation | reactive sulfur species | purple bacteria | Rhodobacter T he discovery of ∼550 deep-sea hydrothermal vents more than 30 y ago (1) has led to the theory that energy metabolism in early ancestral organisms may have arisen from deep-sea hydrothermal vents where simple inorganic molecules such as hydrogen sulfide or hydrogen gas, as well as methane, exist (2-4). Such ancient energy metabolism has been assumed to be similar to that of extant chemolithotrophs, which obtain energy from these molecules. Indeed, various chemolithoautotrophic microbes thrive in deep-sea hydrothermal vents and are capable of oxidizing sulfides, methane, and/or hydrogen gas for use as energy sources and electron donors (5). Some photosynthetic bacteria have also been isolated from deep-sea hydrothermal vents that can grow photosynthetically using sulfide as an electron donor and geothermal radiation as an energy source instead of solar radiation (6), as hypothesized for ancestral phototrophs.Many purple photosynthetic bacteria have remarkable metabolic versatility required to meet the energy demands of sulfidedependent and -independent photosynthesis as well as aerobic and anaerobic respiration. These bacteria tightly control the synthesis of their electron transfer proteins involved in each growth mode in response to a specific electron donor, oxygen tension, and light intensity (7, 8). Among these regulatory systems, oxygen-and lightsensing mechanisms have been well-studied; however, mechanisms used to sen...

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“…Sulfurtransferases are ubiquitously distributed enzymes that function in a range of pathways including sulfur metabolism, iron-sulfur cluster formation, selenium metabolism, and cyanide detoxification (13,14,(25)(26)(27)(28). In humans, there are five sulfurtransferases including mitochondrial rhodanese and MST, which is found in the cytoplasmic and mitochondrial compartments (29,30).…”

Section: Hydrogen Sulfide (H 2 S)mentioning

confidence: 99%

“…Alternatively, the rhodanese domain can be present in a tandem repeat, as in rhodanese and MST, where the active sites are located in a cleft between the N-and C-terminal domains (14,15). Finally, rhodanese domains are fused to other protein domains as in Cdc25 phosphatase (20) or in the PRF and CstB proteins (23,24).Sulfurtransferases are ubiquitously distributed enzymes that function in a range of pathways including sulfur metabolism, iron-sulfur cluster formation, selenium metabolism, and cyanide detoxification (13,14,(25)(26)(27)(28). In humans, there are five sulfurtransferases including mitochondrial rhodanese and MST, which is found in the cytoplasmic and mitochondrial compartments (29,30).…”

mentioning

confidence: 99%

Thiosulfate sulfurtransferase-like domain–containing 1 protein interacts with thioredoxin

Libiad

Motl

Akey

et al. 2018

Journal of Biological Chemistry

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ǂ These authors contributed equally to this work Rhodanese domains are structural modules present in the sulfurtransferase superfamily. These domains can exist as single units, in tandem repeats or fused to domains with other activities. Despite their prevalence across species, the specific physiological roles of most sulfurtransferases are not known. Mammalian rhodanese and mercaptopyruvate sulfurtransferase are perhaps the best-studied members of this protein superfamily and are involved in hydrogen sulfide metabolism. The relatively unstudied human thiosulfate sulfurtransferase like domain-containing 1 (TSTD1) protein, a single-domain cytoplasmic sulfurtransferase, was also postulated to play a role in the sulfide oxidation pathway using thiosulfate to form glutathione persulfide, for subsequent processing in the mitochondrial matrix. Prior kinetic analysis of TSTD1 was performed at pH 9.2, raising questions about relevance and the proposed model for TSTD1 function. In this study, we report a 1.04 Å resolution crystal structure of human TSTD1, which displays an exposed active site that is distinct from that of rhodanese and mercaptopyruvate sulfurtransferase. Kinetic studies with a combination of sulfur donors and acceptors reveal that TSTD1 exhibits a low K M for thioredoxin as a sulfane sulfur acceptor and that it utilizes thiosulfate inefficiently as a sulfur donor. The active site exposure and its interaction with thioredoxin, suggest that TSTD1 might play a role in sulfide-based signaling. The apical localization of TSTD1 in human colonic crypts, which interfaces with sulfide-releasing microbes, and the overexpression of TSTD1 in colon cancer, provides potentially intriguing clues as to its role in sulfide metabolism. Hydrogen sulfide (H 2 S)1 is an important signaling molecule with effects on multiple physiological processes including neuromodulation, inflammation and cardiac function (1-7). Maintaining healthy levels of H 2 S in mammalian cells requires tight control of its biosynthesis and its catabolism (8,9). H 2 S is produced endogenously by two enzymes in the transsulfuration pathway, cystathionine β-synthase and γ-cystathionase as well as by mercaptopyruvate sulfurtransferase (MST) (10-13). H 2 S is oxidized via the sulfide oxidation pathway to generate the end-products thiosulfate Protein persulfidation, a posttranslational modification of cysteine residues, is postulated to be a major mechanism by which H 2 S signals (17). However, the mechanism by which target proteins acquire this modification and the sulfur source(s) used in persulfidation reactions are unclear (18). Sulfurtransferases like rhodanese or the single rhodanese domain containing TSTD1 could potentially play a role in protein persulfidation because of their capacity to form an active site cysteine persulfide during their reaction cycle (18).The rhodanese superfamily members are distinguished by a structural module with an α/β topology in which α-helices surround a central five-stranded β-sheet core (19). At least three variations...

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Common themes and variations in the rhodanese superfamily

Cited by 210 publications

References 52 publications

Rhodanese Functions as Sulfur Supplier for Key Enzymes in Sulfur Energy Metabolism

Rhodanese Functions as Sulfur Supplier for Key Enzymes in Sulfur Energy Metabolism

Sulfide-responsive transcriptional repressor SqrR functions as a master regulator of sulfide-dependent photosynthesis

Thiosulfate sulfurtransferase-like domain–containing 1 protein interacts with thioredoxin

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