- Signaling by hydrogen sulfide and cyanide through posttranslational modification. [Journal Article]
- JEJ Exp Bot 2019 May 14
- A new concept has arisen regarding two cysteine metabolism-related molecules, hydrogen sulfide and hydrogen cyanide, which are considered toxic but have now been established as signaling molecules. H…
A new concept has arisen regarding two cysteine metabolism-related molecules, hydrogen sulfide and hydrogen cyanide, which are considered toxic but have now been established as signaling molecules. Hydrogen sulfide is produced in chloroplasts through the sulfite reductase activity and in the cytosol and mitochondria by the action of sulfide-generating enzymes and regulates/affects essential plant processes such as plant adaptation, development, photosynthesis, autophagy and stomatal movement, where interplay with other signaling molecules occurs. The mechanism of action of sulfide, which modifies protein cysteine thiols to form persulfides, is related to its chemical features. This posttranslational modification, called persulfidation, could play a protective function for thiols against oxidative damage. Hydrogen cyanide is produced during the biosynthesis of ethylene and camalexin in noncyanogenic plants and is detoxified by the action of sulfur-related enzymes. Cyanide functions include the breaking of seed dormancy, modifying the plant responses to biotic stress, and inhibition of root hair elongation. The mode of action of cyanide is under investigation, although it has recently been demonstrated to perform posttranslational modification of protein cysteine thiols to form thiocyanate, a process called S-cyanylation. Therefore, the signaling roles of sulfide and most probably of cyanide are performed through the modification of specific cysteine residues, thus altering protein functions.
- Complete genome sequence of Raoultella sp. strain X13, a promising cell factory for the synthesis of CdS quantum dots. [Journal Article]
- 3B3 Biotech 2019; 9(4):120
- A novel cadmium-resistant bacterium, Raoultella sp. strain X13, recently isolated from heavy metal-contaminated soil, and this strain can synthesize CdS quantum dots using cadmium nitrate [Cd(NO4)2] …
A novel cadmium-resistant bacterium, Raoultella sp. strain X13, recently isolated from heavy metal-contaminated soil, and this strain can synthesize CdS quantum dots using cadmium nitrate [Cd(NO4)2] and l-cysteine. Biomineralization of CdS by strain X13 can efficiently remove cadmium from aqueous solution. To illuminate the molecular mechanisms for the biosynthesis of CdS nanoparticle, the complete genome of Raoultella sp. strain X13 was sequenced. The whole genome sequence comprises a circular chromosome and a circular plasmid. Cysteine desulfhydrase smCSE has been previously found to be associated with the synthesis of CdS quantum dots. Bioinformatics analysis indicated that the genome of Raoultella sp. strain X13 encodes five putative cysteine desulfhydrases and all of them are located in the chromosome. The genome information may help us to determine the molecular mechanisms of the synthesis of CdS quantum dots and potentially enable us to engineer this microorganism for applications in biotechnology.
- Simultaneous bioprecipitation of cadmium to cadmium sulfide nanoparticles and nitrogen fixation by Rhodopseudomonas palustris TN110. [Journal Article]
- CChemosphere 2019; 223:455-464
- This study investigated the abilities of a purple non-sulfur bacterium, Rhodopseudomonas palustris TN110 to bioremediate cadmium through the biosynthesis of CdS nanoparticles and to fix nitrogen simu…
This study investigated the abilities of a purple non-sulfur bacterium, Rhodopseudomonas palustris TN110 to bioremediate cadmium through the biosynthesis of CdS nanoparticles and to fix nitrogen simultaneously. Under microaerobic-light conditions, R. palustris TN110 synthesized CdS nanoparticles. The produced CdS nanoparticles had a spherical shape and an average size of 4.85 nm. The Fourier transform infrared spectrum of the nanoparticles reveals the carbonyl groups, bending vibrations of the amide I and II bands of proteins, and CN stretching vibrations of aromatic and aliphatic amines. These bands and groups suggest protein capping/binding on the surface of the nanoparticles. R. palustris TN110 converted 25.61% of 0.2 mM CdCl2 to CdS nanoparticles under optimal conditions (pH 7.5, 30 °C and 3000 lux). The half maximal inhibitory concentration (IC50) value of the produced CdS nanoparticles was 1.76 mM. The produced CdS nanoparticles at IC50 up-regulated two genes associated with nitrogen fixation: Mo-Fe nitrogenase gene (nifH) and V-Fe nitrogenase gene (vnfG) at 2.83 and 2.27 fold changes, respectively. On the contrary, the produced CdS nanoparticles slightly down-regulated Fe-Fe nitrogenase gene (anfG). The amounts of ammonia released by the strain support the gene expression results. R. palustris TN110 has great potential to serve concurrently as a cadmium bioremediation agent and a nitrogen fixer. The strain could be beneficial to paddy fields that are contaminated with Cd through run off from mining and chemical fertilizer applications.
- Isolation, characterization, and genome insights into an anaerobic sulfidogenic Tissierella bacterium from Cu-bearing coins. [Journal Article]
- AAnaerobe 2019; 56:66-77
- Recent reports on antimicrobial effects of metallic Cu prompted this study of anaerobic microbial communities on copper surfaces. Widely circulating copper-containing coinage was used as a potential …
Recent reports on antimicrobial effects of metallic Cu prompted this study of anaerobic microbial communities on copper surfaces. Widely circulating copper-containing coinage was used as a potential source for microorganisms that had had human contact and were tolerant to copper. This study reports on the isolation, characterization, and genome of an anaerobic sulfidogenic Tissierella sp. P1from copper-containing brass coinage. Dissimilatory (bi)sulfite reductase dsrAB present in strain P1 genome and the visible absorbance around 630 nm in the cells suggested the presence of a desulfoviridin-type protein. However, the sulfate reduction rate measurements with 35SO42- did not confirm the dissimilatory sulfate reduction by the strain. The P1 genome lacks APS reductase, sulfate adenylyltransferase, DsrC, and DsrMK necessary for dissimilatory sulfate reduction. The isolate produced up to 0.79 mM H2S during growth, possibly due to cysteine synthase (CysK) and/or cysteine desulfhydrase (CdsH) activities, encoded in the genome. The strain can tolerate up to 2.4 mM Cu2+(150 mg/l) in liquid medium, shows affinity to metallic copper, and can survive on copper-containing coins up to three days under ambient air and dry conditions. The genome sequence of strain P1 contained cutC, encoding a copper resistance protein, which distinguishes it from all other Tissierella strains with published genomes.
- L-Cysteine production by metabolically engineered Corynebacterium glutamicum. [Journal Article]
- AMAppl Microbiol Biotechnol 2019; 103(6):2609-2619
- L-Cysteine is a commercially important amino acid. Here, we report the construction of L-cysteine-producing Corynebacterium glutamicum using a metabolic engineering approach. L-Serine O-acetyltransfe…
L-Cysteine is a commercially important amino acid. Here, we report the construction of L-cysteine-producing Corynebacterium glutamicum using a metabolic engineering approach. L-Serine O-acetyltransferase (SAT), encoded by cysE gene, is a key enzyme of L-cysteine biosynthesis, because of its feedback inhibition by L-cysteine. Therefore, we introduced a mutation into the C. glutamicum cysE gene, which appeared to desensitize SAT against feedback inhibition by L-cysteine. We successfully produced L-cysteine by overexpressing this mutant cysE gene in C. glutamicum, while the wild-type strain scarcely produced L-cysteine. To enhance the biosynthesis of L-serine (a substrate for SAT), a mutant serA gene, encoding D-3-phosphoglycerate dehydrogenase to desensitize it against feedback inhibition by L-serine, was additionally overexpressed in the mutant cysE-overexpressing strain and its L-cysteine production was indeed improved. Moreover, we disrupted the ldh gene encoding L-lactate dehydrogenase and the aecD gene encoding cysteine desulfhydrase to prevent the formation of lactic acid as a by-product and degradation of L-cysteine produced at the stationary phase, respectively, which resulted in enhanced L-cysteine production. However, since the concentration of L-cysteine produced still decreased at the stationary phase despite the aecD disruption, NCgl2463 encoding a possible cystine importer protein was further disrupted to prevent cystine import, because the produced L-cysteine is immediately oxidized to cystine. As a result, the time before the start of the decrease in L-cysteine concentration was successfully prolonged. Approximately 200 mg/L of L-cysteine production was achieved by overexpression of mutant cysE and serA genes and disruption of aecD and NCgl2463 genes in C. glutamicum.
- L-Cysteine desulfhydrase-dependent hydrogen sulfide is required for methane-induced lateral root formation. [Journal Article]
- PMPlant Mol Biol 2019; 99(3):283-298
- Methane-triggered lateral root formation is not only a universal event, but also dependent on L-cysteine desulfhydrase-dependent hydrogen sulfide signaling. Whether or how methane (CH4) triggers late…
Methane-triggered lateral root formation is not only a universal event, but also dependent on L-cysteine desulfhydrase-dependent hydrogen sulfide signaling. Whether or how methane (CH4) triggers lateral root (LR) formation has not been elucidated. In this report, CH4 induction of lateral rooting and the role of hydrogen sulfide (H2S) were dissected in tomato and Arabidopsis by using physiological, anatomical, molecular, and genetic approaches. First, we discovered that CH4 induction of lateral rooting is a universal event. Exogenously applied CH4 not only triggered tomato lateral rooting, but also increased activities of L-cysteine desulfhydrase (DES; a major synthetic enzyme of H2S) and induced endogenous H2S production, and contrasting responses were observed in the presence of hypotaurine (HT; a scavenger of H2S) or DL-propargylglycine (PAG; an inhibitor of DES) alone. CH4-triggered lateral rooting were sensitive to the inhibition of endogenous H2S with HT or PAG. The changes in the transcripts of representative cell cycle regulatory genes, miRNA and its target genes were matched with above phenotypes. In the presence of CH4, Arabidopsis mutant Atdes1 exhibited defects in lateral rooting, compared with the wild-type. Molecular evidence showed that the transcriptional profiles of representative target genes modulated by CH4 in wild-type plants were impaired in Atdes1 mutant. Overall, our data demonstrate the main branch of the DES-dependent H2S signaling cascade in CH4-triggered LR formation.
- Sodium Hydrosulfide Mitigates Cadmium Toxicity by Promoting Cadmium Retention and Inhibiting Its Translocation from Roots to Shoots in Brassica napus. [Journal Article]
- JAJ Agric Food Chem 2019 Jan 09; 67(1):433-440
- The association between hydrogen sulfide (H2S) and cell wall composition with regard to the mitigation of cadmium (Cd) toxicity in Brassica napus L. was investigated. Cd caused growth retardation, le…
The association between hydrogen sulfide (H2S) and cell wall composition with regard to the mitigation of cadmium (Cd) toxicity in Brassica napus L. was investigated. Cd caused growth retardation, leaf chlorosis, and decreased endogenous H2S content in Brassica napus roots. Stimulating l-cysteine desulfhydrase (LCD)-mediated H2S production with H2S releaser (NaHS) markedly improved plant growth, reduced Cd content in stems and leaves, and rescued Cd-induced chlorosis. Furthermore, increased Cd retention was observed in root cell walls, indicating that NaHS reduced Cd movement from the roots to upper-plant parts. Exogenous NaHS also significantly increased the content of pectin and the activity of pectin methylesterase in cell walls of roots, thereby increasing Cd retention in pectin fractions. However, intensification of H2S barely affected hemicellulose content under Cd stress. Intensified H2S signal, therefore, alleviates Cd toxicity in Brassica napus by increasing pectin content and its demethylation, increasing Cd fixation in cell walls, and reducing root-to-shoot Cd translocation.
- Hydrogen Sulfide-Mediated Activation of O-Acetylserine (Thiol) Lyase and l/d-Cysteine Desulfhydrase Enhance Dehydration Tolerance in Eruca sativa Mill. [Journal Article]
- IJInt J Mol Sci 2018 Dec 11; 19(12)
- Hydrogen sulfide (H₂S) has emerged as an important signaling molecule and plays a significant role during different environmental stresses in plants. The present work was carried out to explore the p…
Hydrogen sulfide (H₂S) has emerged as an important signaling molecule and plays a significant role during different environmental stresses in plants. The present work was carried out to explore the potential role of H₂S in reversal of dehydration stress-inhibited O-acetylserine (thiol) lyase (OAS-TL), l-cysteine desulfhydrase (LCD), and d-cysteine desulfhydrase (DCD) response in arugula (Eruca sativa Mill.) plants. Dehydration-stressed plants exhibited reduced water status and increased levels of hydrogen peroxide (H₂O₂) and superoxide (O₂•-) content that increased membrane permeability and lipid peroxidation, and caused a reduction in chlorophyll content. However, H₂S donor sodium hydrosulfide (NaHS), at the rate of 2 mM, substantially reduced oxidative stress (lower H₂O₂ and O₂•-) by upregulating activities of antioxidant enzymes (superoxide dismutase, peroxidase, and catalase) and increasing accumulation of osmolytes viz. proline and glycine betaine (GB). All these, together, resulted in reduced membrane permeability, lipid peroxidation, water loss, and improved hydration level of plants. The beneficial role of H₂S in the tolerance of plants to dehydration stress was traced with H₂S-mediated activation of carbonic anhydrase activity and enzyme involved in the biosynthesis of cysteine (Cys), such as OAS-TL. H₂S-treated plants showed maximum Cys content. The exogenous application of H₂S also induced the activity of LCD and DCD enzymes that assisted the plants to synthesize more H₂S from accumulated Cys. Therefore, an adequate concentration of H₂S was maintained, that improved the efficiency of plants to mitigate dehydration stress-induced alterations. The central role of H₂S in the reversal of dehydration stress-induced damage was evident with the use of the H₂S scavenger, hypotaurine.
- Characterization of the O-acetylserine(thiol)lyase gene family in Solanum lycopersicum L. [Journal Article]
- PMPlant Mol Biol 2019; 99(1-2):123-134
- This research demonstrated the conservation and diversification of the functions of the O-acetylserine-(thiol) lyase gene family genes in Solanum lycopersicum L. Cysteine is the first sulfur-containi…
This research demonstrated the conservation and diversification of the functions of the O-acetylserine-(thiol) lyase gene family genes in Solanum lycopersicum L. Cysteine is the first sulfur-containing organic molecule generated by plants and is the precursor of many important biomolecules and defense compounds. Cysteine and its derivatives are also essential in various redox signaling-related processes. O-acetylserine(thiol)lyase (OASTL) proteins catalyze the last step of cysteine biosynthesis. Previously, researches focused mainly on OASTL proteins which were the most abundant or possessed the authentic OASTL activity, whereas few studies have ever given a comprehensive view of the functions of all the OASTL members in one specific species. Here, we characterized 8 genes belonging to the OASTL gene family from tomato genome (SlOAS2 to SlOAS9), including the sequence analyses, subcellular localization, enzymatic activity assays, expression patterns, as well as the interaction property with SATs. Apart from SlOAS3, all the other genes encoded OASTL-like proteins. Tomato OASTLs were differentially expressed during the development of tomato plants, and their encoded proteins had diverse compartmental distributions and functions. SlOAS5 and SlOAS6 catalyzed the biogenesis of cysteine in chloroplasts and in the cytosol, respectively, and this was in consistent with their interaction abilities with SlSATs. SlOAS4 catalyzed the generation of hydrogen sulfide, similar to its Arabidopsis ortholog, DES1. SlOAS2 also functioned as an L-cysteine desulfhydrase, but its expression pattern was very different from that of SlOAS4. Additionally, SlOAS8 might be a β-cyanoalanine synthase in mitochondria, and the S-sulfocysteine synthase activity appeared lost in tomato plants. SlOAS7 exhibited a transactivational ability in yeast; while the subcellular localization of SlOAS9 was in the peroxisome and correlated with the process of leaf senescence, indicating that these two genes might have novel roles.
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- Endogenous hydrogen sulfide (H2S) is up-regulated during sweet pepper (Capsicum annuum L.) fruit ripening. In vitro analysis shows that NADP-dependent isocitrate dehydrogenase (ICDH) activity is inhibited by H2S and NO. [Journal Article]
- NONitric Oxide 2018 12 01; 81:36-45
- Like nitric oxide (NO), hydrogen sulfide (H2S) has been recognized as a new gasotransmitter which plays an important role as a signaling molecule in many physiological processes in higher plants. Alt…
Like nitric oxide (NO), hydrogen sulfide (H2S) has been recognized as a new gasotransmitter which plays an important role as a signaling molecule in many physiological processes in higher plants. Although fruit ripening is a complex process associated with the metabolism of reactive oxygen species (ROS) and nitrogen oxygen species (RNS), little is known about the potential involvement of endogenous H2S. Using sweet pepper (Capsicum annuum L.) as a model non-climacteric fruit during the green and red ripening stages, we studied endogenous H2S content and cytosolic l-cysteine desulfhydrase (L-DES) activity which increased by 14% and 28%, respectively, in red pepper fruits. NADPH is a redox compound and key cofactor required for cell growth, proliferation and detoxification. We studied the NADPH-regenerating enzyme, NADP-isocitrate dehydrogenase (NADP-ICDH), whose activity decreased by 34% during ripening. To gain a better understanding of its potential regulation by H2S, we obtained a 50-75% ammonium sulfate-enriched protein fraction containing the NADP-ICDH protein; with the aid of in vitro assays in the presence of H2S, we observed that 2 and 10 mM NaHS used as H2S donors resulted in a decrease of up to 36% and 45%, respectively, in NADP-ICDH activity, which was unaffected by reduced glutathione (GSH). On the other hand, peroxynitrite (ONOO-), S-nitrosocyteine (CysNO) and DETA-NONOate, with the last two acting as NO donors, also inhibited NADP-ICDH activity. In silico analysis of the tertiary structure of sweet pepper NADP-ICDH activity (UniProtKB ID A0A2G2Y555) suggests that residues Cys133 and Tyr450 are the most likely potential targets for S-nitrosation and nitration, respectively. Taken together, the data reveal that the increase in the H2S production capacity of red fruits is due to higher L-DES activity during non-climacteric pepper fruit ripening. In vitro assays appear to show that H2S inhibits NADP-ICDH activity, thus suggesting that this enzyme may be regulated by persulfidation, as well as by S-nitrosation and nitration. NO and H2S may therefore regulate NADPH production and consequently cellular redox status during pepper fruit ripening.