Expression, purification, and &lt;i&gt;S&lt;/i&gt;-nitrosylation of recombinant histone deacetylase 8 in &lt;i&gt;Escherichia coli &lt;/i&gt;

Feng, Jinhong; Jing, Fanbo; Fang, Hao; Gu, Lichuan; Xu, Wenfang

doi:10.5582/bst.2011.v5.1.17

Cited by 22 publications

(19 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…GSNO [30,31]. In those models the oxidation level is typically very high and often performed in denaturing conditions where alterations in protein structure can readily affect the potential of cysteine to undergo modification.…”

Section: Sno/soh Tmt Strategy Detects Endogenous Sno and Soh Levelsmentioning

confidence: 99%

See 1 more Smart Citation

The SNO/SOH TMT strategy for combinatorial analysis of reversible cysteine oxidations

Wojdyła

Williamson

Roepstorff

et al. 2015

Journal of Proteomics

View full text Add to dashboard Cite

SNO/SOH TMT strategy outperforms other available strategies for cysteine oxidation analysis. It provides quantitative profiling of S-nitrosylation and S-sulfenylation changes simultaneously in two experimental conditions. It allows correction of modification levels by protein abundance changes and determination of relative modification site occupancy - all in a single nLC-MSMS experiment based on commercially available reagents. The method has proven precise and sensitive enough to detect and quantify endogenous levels of oxidative stress on proteome-wide scale.

show abstract

Section: Sno/soh Tmt Strategy Detects Endogenous Sno and Soh Levelsmentioning

confidence: 99%

“…In addition to the limitations of existing methods the majority of studies investigating cysteine oxidative modifications use in vitro models where oxidation is induced chemically, for example by treatment with S-nitrosoglutathione (GSNO) [30,31]. Such models do not reflect physiological levels of oxidative modifications.…”

Section: Introductionmentioning

confidence: 99%

The SNO/SOH TMT strategy for combinatorial analysis of reversible cysteine oxidations

Wojdyła

Williamson

Roepstorff

et al. 2015

Journal of Proteomics

View full text Add to dashboard Cite

show abstract

“…HDAC6, which mainly deacetylates cytosolic a-tubulin, is S-nitrosylated by cytokine-induced NO production, resulting in the inhibition of this enzyme (Okuda et al, 2015). Finally, HDAC8 was demonstrated to be modified by NO in vitro (Feng et al, 2011). Interestingly, the catalytic activity of SIRTUIN1 is regulated by reversible S-glutathionylation, which guides vascular development in zebrafish (Bräutigam et al, 2013).…”

Section: Redox Regulation Of Hdacsmentioning

confidence: 99%

“…To explain the observed NO-mediated histone hyperacetylation, we hypothesized that NO might directly target HDACs and inhibit their activity, a mechanism that has been described for some mammalian HDACs (Colussi et al, 2008;Nott et al, 2008;Feng et al, 2011;Okuda et al, 2015). To determine the effect of NO on histone deacetylase activity, a commercial fluorescence-based HDAC assay was modified to be used in protoplasts.…”

Section: Hdac Activity Is Inhibited By Redox Modificationsmentioning

confidence: 99%

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

et al. 2016

View full text Add to dashboard Cite

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.

show abstract

“…The activity of class I enzymes HDAC 2 and 8 has been reported to be directly inhibited by NO-dependent S-nitrosylation. 25,26 S-Nitrosylation of HDAC2 induces its release from chromatin. 27 The nuclear shuttling of class IIa HDACs is also induced by NO through the sGC– cGMP pathway.…”

Section: Introductionmentioning

confidence: 99%

Design, Synthesis, and Antitumor Evaluation of Novel Histone Deacetylase Inhibitors Equipped with a Phenylsulfonylfuroxan Module as a Nitric Oxide Donor

Duan

Inks

et al. 2015

J. Med. Chem.

Self Cite

View full text Add to dashboard Cite

On the basis of the strategy of creating multifunctional drugs, a novel series of phenylsulfonylfuroxan-based hydroxamates with histone deacetylase (HDAC) inhibitory and nitric oxide (NO) donating activities were designed, synthesized, and evaluated. The most potent NO donor–HDAC inhibitor (HDACI) hybrid, 5c, exhibited a much greater in vitro antiproliferative activity against the human erythroleukemia (HEL) cell line than that of the approved drug SAHA (Vorinostat), and its antiproliferative activity was diminished by the NO scavenger hemoglobin in a dose-dependent manner. Further mechanism studies revealed that 5c strongly induced cellular apoptosis and G1 phase arrest in HEL cells. Animal experiment identified 5c as an orally active agent with potent antitumor activity in a HEL cell xenograft model. Interestingly, although compound 5c was remarkably HDAC6-selective at the molecular level, it exhibited pan-HDAC inhibition in a western blot assay, which is likely due to class I HDACs inhibition caused by NO release at the cellular level.

show abstract

Expression, purification, and <i>S</i>-nitrosylation of recombinant histone deacetylase 8 in <i>Escherichia coli </i>

Cited by 22 publications

References 22 publications

The SNO/SOH TMT strategy for combinatorial analysis of reversible cysteine oxidations

The SNO/SOH TMT strategy for combinatorial analysis of reversible cysteine oxidations

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

Design, Synthesis, and Antitumor Evaluation of Novel Histone Deacetylase Inhibitors Equipped with a Phenylsulfonylfuroxan Module as a Nitric Oxide Donor

Contact Info

Product

Resources

About