scholarly journals Molecular Mechanism of Ethanol Fermentation Inhibition via Protein Tyrosine Nitration of Pyruvate Decarboxylase by Reactive Nitrogen Species in Yeast

2022 ◽  
Author(s):  
Supapid Eknikom ◽  
Ryo Nasuno ◽  
Hiroshi Takagi
Keyword(s):  
Ethanol Production ◽  
Reactive Nitrogen Species ◽  
Pyruvate Decarboxylase ◽  
Inhibitory Effect ◽  
Yeast Cells ◽  
Reactive Nitrogen ◽  
Tyrosine Nitration ◽  
Nitrogen Species ◽  
Protein Tyrosine ◽  
Protein Tyrosine Nitration

Abstract Protein tyrosine nitration (PTN), in which tyrosine (Tyr) residues on proteins are converted into 3-nitrotyrosine (NT), is one of the post-translational modifications mediated by reactive nitrogen species (RNS). Many recent studies have reported that PTN contributed to signaling systems by altering the structures and/or functions of proteins. This study aimed to investigate connections between PTN and the inhibitory effect of nitrite-derived RNS on fermentation ability using the yeast Saccharomyces cerevisiae. The results indicated that RNS inhibited the ethanol production of yeast cells with increased intracellular pyruvate content. We also found that RNS decreased the activities of pyruvate decarboxylase (PDC) as a critical enzyme involved in ethanol production. Our proteomic analysis revealed that the main PDC isozyme Pdc1 underwent the PTN modification at Tyr38, Tyr157, and Tyr344. The biochemical analysis using the recombinant purified Pdc1 enzyme indicated that PTN at Tyr157 or Tyr344 significantly reduced the Pdc1 activity. Interestingly, the substitution of Tyr157 or Tyr344 to phenylalanine, which is no longer converted into NT, recovered the ethanol production under the RNS treatment conditions. These findings suggest that nitrite impairs the fermentation ability of yeast by inhibiting the Pdc1 activity via its PTN modification at Tyr157 and Tyr344 of Pdc1.

Protein Tyrosine Nitration Induced by Heme/Hydrogen Peroxide: Inhibitory Effect of Hydroxycinnamoyl Conjugates

Planta Medica ◽  
2006 ◽  
Vol 73 (01) ◽  
pp. 20-26 ◽  
Author(s):  
Ana Olmos ◽  
Salvador Máñez ◽  
Rosa Giner ◽  
M. Recio ◽  
José Ríos
Keyword(s):  
Hydrogen Peroxide ◽  
Inhibitory Effect ◽  
Tyrosine Nitration ◽  
Protein Tyrosine ◽  
Protein Tyrosine Nitration

scholarly journals The reactive nitrogen species peroxynitrite is a potent inhibitor of renal Na-K-ATPase activity

2008 ◽  
Vol 295 (4) ◽  
pp. F1191-F1198 ◽  
Author(s):  
Matthew S. Reifenberger ◽  
Krista L. Arnett ◽  
Craig Gatto ◽  
Mark A. Milanick
Keyword(s):  
Atpase Activity ◽  
Reactive Nitrogen Species ◽  
Potent Inhibitor ◽  
In Vivo Studies ◽  
Reactive Nitrogen ◽  
Tyrosine Nitration ◽  
Nitrogen Species ◽  
Single Bolus ◽  
Atpase Inhibition

Peroxynitrite is a reactive nitrogen species produced when nitric oxide and superoxide react. In vivo studies suggest that reactive oxygen species and, perhaps, peroxynitrite can influence Na-K-ATPase function. However, the direct effects of peroxynitrite on Na-K-ATPase function remain unknown. We show that a single bolus addition of peroxynitrite inhibited purified renal Na-K-ATPase activity, with IC50 of 107 ± 9 μM. To mimic cellular/physiological production of peroxynitrite, a syringe pump was used to slowly release (∼0.85 μM/s) peroxynitrite. The inhibition of Na-K-ATPase activity induced by this treatment was similar to that induced by a single bolus addition of equal cumulative concentration. Peroxynitrite produced 3-nitrotyrosine residues on the α, β, and FXYD subunits of the Na pump. Interestingly, the flavonoid epicatechin, which prevented tyrosine nitration, was unable to blunt peroxynitrite-induced ATPase inhibition, suggesting that tyrosine nitration is not required for inhibition. Peroxynitrite led to a decrease in iodoacetamidofluorescein labeling, implying that cysteine modifications were induced. Glutathione was unable to reverse ATPase inhibition. The presence of Na+ and low MgATP during peroxynitrite treatment increased the IC50 to 145 ± 10 μM, while the presence of K+ and low MgATP increased the IC50 to 255 ± 13 μM. This result suggests that the EPNa conformation of the pump is slightly more sensitive to peroxynitrite than the E(K) conformation. Taken together, these results show that peroxynitrite is a potent inhibitor of Na-K-ATPase activity and that peroxynitrite can induce amino acid modifications to the pump.

scholarly journals Different Nitro-Oxidative Response of Odontarrhena lesbiaca Plants from Geographically Separated Habitats to Excess Nickel

Antioxidants ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 837
Author(s):  
Gábor Feigl ◽  
Viktória Varga ◽  
Árpád Molnár ◽  
Panayiotis G. Dimitrakopoulos ◽  
Zsuzsanna Kolbert
Keyword(s):  
Reactive Nitrogen Species ◽  
Dry Weight ◽  
Serpentine Soils ◽  
Tyrosine Nitration ◽  
Tolerance Mechanisms ◽  
Protein Tyrosine ◽  
Protein Tyrosine Nitration ◽  
Relative Tolerance ◽  
Study Sites ◽  
The Relationship

Odontarrhena lesbiaca is an endemic species to the serpentine soils of Lesbos Island (Greece). As a nickel (Ni) hyperaccumulator, it possesses an exceptional Ni tolerance; and it can accumulate up to 0.2–2.4% Ni of its leaves’ dry weight. In our study, O. lesbiaca seeds from two geographically separated study sites (Ampeliko and Loutra) were germinated and grown on control and Ni-containing (3000 mg/kg) soil in a rhizotron system. Ni excess induced significant Ni uptake and translocation in both O. lesbiaca ecotypes and affected their root architecture differently: plants from the Ampeliko site proved to be more tolerant; since their root growth was less inhibited compared to plants originated from the Loutra site. In the roots of the Ampeliko ecotype nitric oxide (NO) was being accumulated, while the degree of protein tyrosine nitration decreased; suggesting that NO in this case acts as a signaling molecule. Moreover, the detected decrease in protein tyrosine nitration may serve as an indicator of this ecotype’s better relative tolerance compared to the more sensitive plants originated from Loutra. Results suggest that Ni hypertolerance and the ability of hyperaccumulation might be connected to the plants’ capability of maintaining their nitrosative balance; yet, relatively little is known about the relationship between excess Ni, tolerance mechanisms and the balance of reactive nitrogen species in plants so far.

Evidence for peroxynitrite as a signaling molecule in flow-dependent activation of c-Jun NH2-terminal kinase

1999 ◽  
Vol 277 (4) ◽  
pp. H1647-H1653 ◽  
Author(s):  
Young-Mi Go ◽  
Rakesh P. Patel ◽  
Matthew C. Maland ◽  
Heonyong Park ◽  
Joseph S. Beckman ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Shear Stress ◽  
Protein Kinase ◽  
Reactive Nitrogen Species ◽  
Mitogen Activated Protein Kinase ◽  
Reactive Nitrogen ◽  
Tyrosine Nitration ◽  
Nitrogen Species ◽  
Laminar Shear Stress ◽  
As Stress

The c-Jun NH2-terminal kinase (JNK), also known as stress-activated protein kinase, is a mitogen-activated protein kinase that determines cell survival in response to environmental stress. Activation of JNK involves redox-sensitive mechanisms and physiological stimuli such as shear stress, the dragging force generated by blood flow over the endothelium. Laminar shear stress has antiatherogenic properties and controls structure and function of endothelial cells by mechanisms including production of nitric oxide (NO) and superoxide ([Formula: see text]). Here we show that both NO and [Formula: see text] are required for activation of JNK by shear stress in endothelial cells. The present study also demonstrates that exposure of endothelial cells to shear stress increases tyrosine nitration, a marker of reactive nitrogen species formation. Furthermore, inhibitors or scavengers of NO, [Formula: see text], or reactive nitrogen species prevented shear-dependent increase in tyrosine nitration and activation of JNK. Peroxynitrite alone, added to cells as a bolus or generated over 60 min by 3-morpholinosydnonimine, also activates JNK. These results suggest that reactive nitrogen species, in this case most likely peroxynitrite, act as signaling molecules in the mechanoactivation of JNK.

Reactive Nitrogen Species and Tyrosine Nitration in the Respiratory Tract

1999 ◽  
Vol 160 (1) ◽  
pp. 1-9 ◽  
Author(s):  
ALBERT van der VLIET ◽  
JASON P. EISERICH ◽  
MARK K. SHIGENAGA ◽  
CARROLL E. CROSS
Keyword(s):  
Respiratory Tract ◽  
Reactive Nitrogen Species ◽  
Reactive Nitrogen ◽  
Tyrosine Nitration ◽  
Nitrogen Species
Sign in / Sign up

Export Citation Format

Share Document