Regulation of plant cytosolic aldolase functions by redox-modifications

Linde, Karina van der; Gutsche, Nora; Leffers, Hans-Martin; Lindermayr, Christian; Müller, Bernd; Holtgrefe, Simone; Scheibe, Renate

doi:10.1016/j.plaphy.2011.06.009

Cited by 59 publications

(51 citation statements)

References 52 publications

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“…This is supported by other reports that demonstrated transcriptional alterations of metabolic enzymes in response to GSNO (Begara-Morales et al, 2014). Moreover, NO might affect the activity of a variety of enzymes involved in cellular metabolism by posttranslational mechanisms (Holtgrefe et al, 2008;Palmieri et al, 2010;van der Linde et al, 2011). Together, these data suggest that GSNO induces a metabolic shift in the cell, which is the result of transcriptional as well as posttranslational regulation of metabolic enzymes.…”

Section: Possible Role Of No-mediated H3k9/14ac Changes During the Desupporting

confidence: 84%

Nitric Oxide Modulates Histone Acetylation at Stress Genes by Inhibition of Histone Deacetylases

et al. 2016

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Histone acetylation, which is an important mechanism to regulate gene expression, is controlled by the opposing action of histone acetyltransferases and histone deacetylases (HDACs). In animals, several HDACs are subjected to regulation by nitric oxide (NO); in plants, however, it is unknown whether NO affects histone acetylation. We found that treatment with the physiological NO donor S-nitrosoglutathione (GSNO) increased the abundance of several histone acetylation marks in Arabidopsis (Arabidopsis thaliana), which was strongly diminished in the presence of the NO scavenger 2-4-carboxyphenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide. This increase was likely triggered by NO-dependent inhibition of HDAC activity, since GSNO and S-nitroso-N-acetyl-DL-penicillamine significantly and reversibly reduced total HDAC activity in vitro (in nuclear extracts) and in vivo (in protoplasts). Next, genome-wide H3K9/14ac profiles in Arabidopsis seedlings were generated by chromatin immunoprecipitation sequencing, and changes induced by GSNO, GSNO/2-4-carboxyphenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide or trichostatin A (an HDAC inhibitor) were quantified, thereby identifying genes that display putative NO-regulated histone acetylation. Functional classification of these genes revealed that many of them are involved in the plant defense response and the abiotic stress response. Furthermore, salicylic acid, which is the major plant defense hormone against biotrophic pathogens, inhibited HDAC activity and increased histone acetylation by inducing endogenous NO production. These data suggest that NO affects histone acetylation by targeting and inhibiting HDAC complexes, resulting in the hyperacetylation of specific genes. This mechanism might operate in the plant stress response by facilitating the stress-induced transcription of genes.

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Section: Possible Role Of No-mediated H3k9/14ac Changes During the Desupporting

confidence: 84%

Nitric Oxide Modulates Histone Acetylation at Stress Genes by Inhibition of Histone Deacetylases

et al. 2016

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“…Compared with previous S-nitrosoproteomic studies in Arabidopsis (Lindermayr et al, 2005;Romero-Puertas et al, 2008;Palmieri et al, 2010;Fares et al, 2011;Puyaubert et al, 2014), we found that 42.6% (72/169) of those previously reported S-nitrosylated proteins were also identified in our site-specific analysis, including the aforementioned SABP3, FBA6, and APX1 (see Supplemental Table S5). For example, Cys-173 of FBA6 was previously characterized as an S-nitrosylation site (van der Linde et al, 2011), and this site was also identified by our site-specific proteomic analysis ( Fig. 1E; Supplemental Table S5).…”

Section: Site-specific Identification Of S-nitrosylated Proteins In Csupporting

confidence: 57%

“…In particular, three previously characterized S-nitrosylated proteins, SABP3 (also known as carbonic anhydrase1 [CA1]; Wang et al, 2009), Fru 1,6-bisphosphate aldolase 6 (FBA6; van der Linde et al, 2011), and ascorbate peroxidase1 (APX1; CorreaAragunde et al, 2013), were identified in our S-nitrosoproteomic analysis (see Supplemental Table S1). S-nitrosylation of SABP3 suppresses its binding with salicylic acid and the enzymatic activity during the hypersensitive response, whereas S-nitrosylation of FBA6 negatively regulates its enzymatic activity van der Linde et al, 2011).…”

Section: Resultsmentioning

confidence: 84%

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Site-Specific Nitrosoproteomic Identification of EndogenouslyS-Nitrosylated Proteins in Arabidopsis

et al. 2015

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Nitric oxide (NO) regulates multiple developmental events and stress responses in plants. A major biologically active species of NO is S-nitrosoglutathione (GSNO), which is irreversibly degraded by GSNO reductase (GSNOR). The major physiological effect of NO is protein S-nitrosylation, a redox-based posttranslational modification mechanism by covalently linking an NO molecule to a cysteine thiol. However, little is known about the mechanisms of S-nitrosylation-regulated signaling, partly due to limited S-nitrosylated proteins being identified. In this study, we identified 1,195 endogenously S-nitrosylated peptides in 926 proteins from the Arabidopsis (Arabidopsis thaliana) by a site-specific nitrosoproteomic approach, which, to date, is the largest data set of S-nitrosylated proteins among all organisms. Consensus sequence analysis of these peptides identified several motifs that contain acidic, but not basic, amino acid residues flanking the S-nitrosylated cysteine residues. These S-nitrosylated proteins are involved in a wide range of biological processes and are significantly enriched in chlorophyll metabolism, photosynthesis, carbohydrate metabolism, and stress responses. Consistently, the gsnor1-3 mutant shows the decreased chlorophyll content and altered photosynthetic properties, suggesting that S-nitrosylation is an important regulatory mechanism in these processes. These results have provided valuable resources and new clues to the studies on S-nitrosylation-regulated signaling in plants.

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“…Evidences for NO accumulation in the nucleus of stomatal and epidermal cells in response to various stress conditions like heat, green light, osmotic stress, and elicitors has been reported [26][27][28]. Moreover, S-nitrosylation has been studied in some nuclearlocalized proteins such as Non-expressor of Pathogenesis-related genes 1 (NPR1), transcription factor TGA1, glyceraldehyde-3-phosphate dehydrogenase, aldolase, and MYB transcription factors [29][30][31][32].…”

Section: Introductionmentioning

confidence: 99%

Identification of nuclear target proteins for S-nitrosylation in pathogen-treated Arabidopsis thaliana cell cultures

et al. 2015

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Regulation of plant cytosolic aldolase functions by redox-modifications

Cited by 59 publications

References 52 publications

Nitric Oxide Modulates Histone Acetylation at Stress Genes by Inhibition of Histone Deacetylases

Nitric Oxide Modulates Histone Acetylation at Stress Genes by Inhibition of Histone Deacetylases

Site-Specific Nitrosoproteomic Identification of EndogenouslyS-Nitrosylated Proteins in Arabidopsis

Identification of nuclear target proteins for S-nitrosylation in pathogen-treated Arabidopsis thaliana cell cultures

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