PDC | Pyruvate decarboxylase
AS10 691 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A. thaliana, O. sativa, Z. mobilis
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65 | 65 kDa (Arabidopsis thaliana)
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Reactant: Arabidopsis thaliana (Thale cress)
Application: Western Blotting
Pudmed ID: 25226037
Journal: PLoS Biol
Figure Number: 3D
Published Date: 2014-09-01
First Author: Giuntoli, B., Lee, S. C., et al.
Impact Factor: 7.279Open Publication
HRA1 contributes to plant submergence survival.(A) Effect of HRA1 misexpression on rosette growth in air, or after recovery from 72 h submergence in darkness. Scale bar, 2 cm. (B) Percentage of plants surviving flooding-induced hypoxia (n?=?5), dry weight of rosette plants kept under control growth conditions (n?=?6), and dry weight of rosettes after postsubmergence recovery (n?=?6). Data are mean ± s.d.; *p<0.05, significant differences from the wild type after one-way ANOVA. (C) HRA1 regulates target gene transcripts in an age-dependent manner in leaves of plants treated with complete submergence. Transcripts were measured before submergence (“control conditions”), after 4 h submergence in darkness (“submergence”), and after 1 h de-submergence in the light (“reoxygenation”). Relative transcript values were calculated using old leaves of the wild type under control conditions as the reference sample. Data are mean ± s.d. (n?=?3); letters indicate statistically significant differences between genotypes after one-way ANOVA (p<0.05) performed independently on each leaf type. (D) Western blot analysis of ADH and PDC protein accumulation in leaves at different developmental stages from control and submerged (4 h) plants. The full-size images of the hybridized membranes can be found in Figure S10. (E) Stability of the translational fusion RAP2.12:RrLuc protein (RrLuc, Renilla reniformis luciferase) in Arabidopsis mesophyll protoplasts upon transfection with increasing amounts of 35S:HRA1. RAP2.12:RrLuc abundance was evaluated from the RrLuc relative activity, measured through a dual luciferase assay. Data are mean ± s.d. (n?=?4), and the asterisks indicate statistically significant differences (p<0.05) from protoplasts expressing RAP2.12:RrLuc alone, after one-way ANOVA.
Pyruvate decarboxylase (PDC) is a homotetrameric enzyme (E.C.220.127.116.11) that catalyses the decarboxylation of pyruvic acid to acetaldehyde carbon dioxide in the cytoplasm. It is also called 2-oxo-acid carboxylase, and pyruvic decarboxylase. In anaerobic conditions, this enzyme is part of the fermentation process that occurs in yeast, especially the Saccharomyces genus, to produce ethanol by fermentation. Pyruvate decarboxylase starts this process by converting pyruvate into acetaldehyde and carbon dioxide. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. This enzyme should not be mistaken for the unrelated enzyme pyruvate dehydrogenase, an oxidoreductase (EC 18.104.22.168), that catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA.
Gil-Monreal et al. (2019). ERF-VII transcription factors induce ethanol fermentation in response to amino acid biosynthesis-inhibiting herbicides. J Exp Bot. 2019 Aug 6. pii: erz355. doi: 10.1093/jxb/erz355.
Giuntoli et al. (2014). A trihelix DNA binding protein counterbalances hypoxia-responsive transcriptional activation in Arabidopsis. PLoS Biol. 2014 Sep 16;12(9):e1001950. doi: 10.1371/journal.pbio.1001950. eCollection 2014.
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