Growth and Hydrogen Sulfide Emission of Photoheterotrophic Tobacco Cells Supplied with L-cysteine as Sole Sulfur Source

1985 ◽  
Vol 120 (1) ◽  
pp. 47-56 ◽  
Author(s):  
Heinz Rennenberg ◽  
Ina Grundel
Keyword(s):  
Hydrogen Sulfide ◽  
Sulfur Source ◽  
Tobacco Cells

Degradation of Glutathione in Plant Cells: Evidence against the Participation of a γ-Glutamyltranspeptidase

1985 ◽  
Vol 40 (1-2) ◽  
pp. 29-33 ◽  
Author(s):  
Reinhard Steinkamp ◽  
Heinz Rennenberg
Keyword(s):  
Ammonium Sulfate ◽  
Plant Cells ◽  
Artificial Substrate ◽  
Sulfur Source ◽  
Tobacco Cell ◽  
Tobacco Cells ◽  
Assay Mixture ◽  
Feeding Experiments ◽  
Low Rate

When γ-glutamyltranspeptidase activity in tobacco cells was measured using the artificial substrate γ-glutamyl-p-nitroanilide, liberation of p-nitroaniline was not reduced, but stimulated by addition of glutathione. Therefore, glutathione was not acting as a donator, but as an acceptor of γ-glutamyl moieties in the assay mixture, suggesting that γ-glutamvltranspeptidase is not participating in degradation of glutathione. Feeding experiments with [35S-cys]glutathione sup­ported this conclusion. When tobacco cells were supplied with this peptide as sole sulfur source, glutathione and γ-glutamylcysteine were the only labelled compounds found inside the cells. The low rate of uptake of glutathione apparently prevented the accumulation of measurable amounts of radioactivity in the cysteine pool. A γ-glutamylcyclotransferase, responsible for the conversion of γ-glutamylcysteine to 5-oxo-proline and cysteine was found in ammonium sulfate precipitates of tobacco cell homogenates. The enzyme showed high activities with γ-glutamylmethionine and γ-glutamylcysteine, but not with other γ-glutamyldipeptides or glutathione. From these and previously published experiments [(Rennenberg et a!., Z. Naturforsch. 35c, 708-711 (1980)], it is concluded that glutathione is degraded in tobacco cells via the following pathway: γ-glu-cys-gly → γ-glu-cys → 5-oxo-proline → glu.

Evidence for the Participation of a 5-Oxo-prolinase in Degradation of Glutathione in Nicotiana tabacum

1980 ◽  
Vol 35 (9-10) ◽  
pp. 708-711 ◽  
Author(s):  
Heinz Rennenberg ◽  
Reinhard Steinkamp ◽  
Andrea Polle
Keyword(s):  
Nicotiana Tabacum ◽  
Glutamic Acid ◽  
Suspension Cultures ◽  
Sulfur Source ◽  
Tobacco Cells ◽  
Tobacco Suspension Cultures

Abstract During degradation of glutathione in tobacco suspension cultures substancial amounts of 5-oxo-proline are formed in vivo as well as in crude cell homogenates in vitro. The existance of a 5-oxo-prolinase that catalyzes the conversion of 5-oxo-proline to glutamic acid was demonstrated in tobacco cells, grown with glutathione as sole sulfur source.

Effects of dietary sulfur source on rumen pH and hydrogen sulfide gas concentration

2014 ◽  
Vol 165 ◽  
pp. 66-69 ◽  
Author(s):  
M.E. Drewnoski ◽  
C.J. Brasche ◽  
S.L. Hansen
Keyword(s):  
Hydrogen Sulfide ◽  
Sulfur Source ◽  
Gas Concentration ◽  
Rumen Ph

scholarly journals Atmospheric H2S exposure does not affect stomatal aperture in maize

Planta ◽  
2020 ◽  
Vol 252 (4) ◽  
Author(s):  
Ties Ausma ◽  
Jeffrey Mulder ◽  
Thomas R. Polman ◽  
Casper J. van der Kooi ◽  
Luit J. De Kok
Keyword(s):  
Hydrogen Sulfide ◽  
Transpiration Rate ◽  
Stomatal Density ◽  
Stomatal Closure ◽  
Stomatal Resistance ◽  
Stomatal Aperture ◽  
Sulfur Source ◽  
Growth Reduction ◽  
Signal Molecule ◽  
Lower Biomass

Abstract Main conclusion Stomatal aperture in maize is not affected by exposure to a subtoxic concentration of atmospheric H2S. At least in maize, H2S, thus, is not a gaseous signal molecule that controls stomatal aperture. Abstract Sulfur is an indispensable element for the physiological functioning of plants with hydrogen sulfide (H2S) potentially acting as gasotransmitter in the regulation of stomatal aperture. It is often assumed that H2S is metabolized into cysteine to stimulate stomatal closure. To study the significance of H2S for the regulation of stomatal closure, maize was exposed to a subtoxic atmospheric H2S level in the presence or absence of a sulfate supply to the root. Similar to other plants, maize could use H2S as a sulfur source for growth. Whereas sulfate-deprived plants had a lower biomass than sulfate-sufficient plants, exposure to H2S alleviated this growth reduction. Shoot sulfate, glutathione, and cysteine levels were significantly higher in H2S-fumigated plants compared to non-fumigated plants. Nevertheless, this was not associated with changes in the leaf area, stomatal density, stomatal resistance, and transpiration rate of plants, meaning that H2S exposure did not affect the transpiration rate per stoma. Hence, it did not affect stomatal aperture, indicating that, at least in maize, H2S is not a gaseous signal molecule controlling this aperture.

scholarly journals A novel deep-sea bacterial threonine dehydratase drives cysteine desulfuration and hydrogen sulfide production

2020 ◽  
Author(s):  
Ning Ma ◽  
Yufan Sun ◽  
Wen Zhang ◽  
Chaomin Sun
Keyword(s):  
Hydrogen Sulfide ◽  
Active Site ◽  
Deep Sea ◽  
Sulfur Source ◽  
Broad Distribution ◽  
Threonine Dehydratase ◽  
Sulfide Production ◽  
Hydrogen Sulfide Production

ABSTRACTCysteine desulfuration is one of the main ways for hydrogen sulfide (H2S) generation in cells and is usually conducted by cystathionine γ-lyase. Herein, we describe a newly discovered deep-sea bacterial threonine dehydratase (psTD), which is surprisingly discovered to drive L-cysteine desulfuration. The mechanisms of psTD catalyzing cysteine desulfuration towards H2S production are first clarified in vitro and in vivo through a combination of genetic and biochemical methods. Furthermore, based on the solved structures of psTD and its various mutants, two or three pockets are found in the active site of psTD, and switch states between inward and outward orientation of a key amino acid R77 determine the open or close status of Pocket III for small molecule exchanges, which further facilitates cysteine desulfuration. Our results reveal the functional diversity and structural specificity of psTD towards L-cysteine desulfuration and H2S formation. Given the broad distribution of psTD homologs in different bacteria, we speculate that some threonine dehydratases have evolved a novel function towards cysteine desulfuration, which benefits the producer to utilize cysteine as a sulfur source for better adapting external environments.

Hydrogen Sulfide Emission by Cultured Tobacco Cells

1983 ◽  
Vol 111 (3) ◽  
pp. 189-202 ◽  
Author(s):  
Heinz Rennenberg ◽  
Georg Reski ◽  
Andrea Polle
Keyword(s):  
Hydrogen Sulfide ◽  
Tobacco Cells

Endogenous hydrogen sulfide sulfhydrates IKKβ at cysteine 179 to control pulmonary artery endothelial cell inflammation

2019 ◽  
Vol 133 (20) ◽  
pp. 2045-2059 ◽  
Author(s):  
Da Zhang ◽  
Xiuli Wang ◽  
Siyao Chen ◽  
Selena Chen ◽  
Wen Yu ◽  
...  
Keyword(s):  
Hydrogen Sulfide ◽  
Endothelial Cell ◽  
Pulmonary Artery ◽  
Cell Model ◽  
Site Directed Mutagenesis ◽  
Critical Event ◽  
Hypertensive Rats ◽  
Pulmonary Artery Endothelial Cell

Abstract Background: Pulmonary artery endothelial cell (PAEC) inflammation is a critical event in the development of pulmonary arterial hypertension (PAH). However, the pathogenesis of PAEC inflammation remains unclear. Methods: Purified recombinant human inhibitor of κB kinase subunit β (IKKβ) protein, human PAECs and monocrotaline-induced pulmonary hypertensive rats were employed in the study. Site-directed mutagenesis, gene knockdown or overexpression were conducted to manipulate the expression or activity of a target protein. Results: We showed that hydrogen sulfide (H2S) inhibited IKKβ activation in the cell model of human PAEC inflammation induced by monocrotaline pyrrole-stimulation or knockdown of cystathionine γ-lyase (CSE), an H2S generating enzyme. Mechanistically, H2S was proved to inhibit IKKβ activity directly via sulfhydrating IKKβ at cysteinyl residue 179 (C179) in purified recombinant IKKβ protein in vitro, whereas thiol reductant dithiothreitol (DTT) reversed H2S-induced IKKβ inactivation. Furthermore, to demonstrate the significance of IKKβ sulfhydration by H2S in the development of PAEC inflammation, we mutated C179 to serine (C179S) in IKKβ. In purified IKKβ protein, C179S mutation of IKKβ abolished H2S-induced IKKβ sulfhydration and the subsequent IKKβ inactivation. In human PAECs, C179S mutation of IKKβ blocked H2S-inhibited IKKβ activation and PAEC inflammatory response. In pulmonary hypertensive rats, C179S mutation of IKKβ abolished the inhibitory effect of H2S on IKKβ activation and pulmonary vascular inflammation and remodeling. Conclusion: Collectively, our in vivo and in vitro findings demonstrated, for the first time, that endogenous H2S directly inactivated IKKβ via sulfhydrating IKKβ at Cys179 to inhibit nuclear factor-κB (NF-κB) pathway activation and thereby control PAEC inflammation in PAH.

Increased N-acylphosphatidylethanolamine biosynthesis in elicitor-treated tobacco cells

1995 ◽  
Vol 95 (1) ◽  
pp. 120-126 ◽  
Author(s):  
Kent D. Chapman ◽  
Allison Conyers-Jackson ◽  
Robert A. Moreau ◽  
Swati Tripathy
Keyword(s):  
Tobacco Cells
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