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Nitric oxide-mediated s-nitrosylation of IAA17 protein in intrinsically disordered region represses auxin signaling

Journal of Genetics and Genomics 2023年第7期50卷 473-485页

作者： Hongwei Jing Xiaolu Yang Ryan J.Emenecker Jian Feng Jian Zhang Marcelo Rodrigues Alves de Figueiredo Patarasuda Chaisupa R.Clay Wright Alex s.Holehouse Lucia C.strader Jianru Zuo state Key Laboratory of Plant Genomics Institute of Genetics and Developmental BiologyChinese Academy of SciencesBeijing 100101China University of Chinese Academy of sciences Beijing 100049China Department of Biology Duke UniversityDurhamNC 27008USA Department of Neurobiology Duke University Medical CenterDurhamNC 27710USA Department of Biochemistry and Molecular Biophysics Washington University School of MedicineSt.LouisMO 63110USA Center for Biomolecular Condensates(CBC) Washington University in St.LouisSt.LouisMO 63130USA Department of Biological systems Engineering Virginia TechBlacksburgVA 24061USA The Translational Plant sciences Center(TPsC) Virginia TechBlacksburgVA 24061USA CAs Center for Excellence in Molecular Plant sciences Chinese Academy of SciencesBeijing 100101China

The phytohormone auxin plays crucial roles in nearly every aspect of plant growth and development.Auxin signaling is activated through the phytohormone-induced proteasomal degradation of the Auxin/INDOLE-3-ACETIC ACID(Aux/IAA)family of transcriptional repressors.Notably,many auxin-modulated physiological processes are also regulated by nitric oxide(NO)that executes its biological effects predominantly through protein s-nitrosylation at specific cysteine residues.However,little is known about the molecular mechanisms in regulating the interactive NO and auxin networks.Here,we show that NO represses auxin signaling by inhibiting IAA17 protein degradation.NO induces the s-nitrosylation of Cys-70 located in the intrinsically disordered region of IAA17,which inhibits the TIR1-IAA17 interaction and consequently the proteasomal degradation of IAA17.The accumulation of a higher level of IAA17 attenuates auxin response.Moreover,an IAA17^(C70W)nitrosomimetic mutation renders the accumulation of a higher level of the mutated protein,thereby causing partial resistance to auxin and defective lateral root development.Taken together,these results suggest that s-nitrosylation of IAA17 at Cys-70 inhibits its interaction with TIR1,thereby negatively regulating auxin signaling.This study provides unique molecular insights into the redox-based auxin signaling in regulating plant growth and development.

关键词： Arabidopsis thaliana Auxin Aux/IAA Nitric oxide s-nitrosylation Intrinsically disordered region

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An Insight of s-nitrosylation of Human GIF

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Chinese Journal of Chemistry 2005年第11期23卷 1545-1551页

作者： TENG, Xin-Chen ZHENG, Qi CAI, Bin NI, Feng-Yun XlE, yi sUN, Hong-Zhe ZHANG, Ming-Jie HUANG, Zhong-Xian Department of Chemistry Institute of Genetics Life Science School Fudan University Shanghai 200433 China Department of Chemistry The University of Hong Kong Pokfulam Road Hong Kong China Department of Biochemistry Hong Kong University of Science and Technology Clear Water Bay Kowloon Hong Kong China

Neural growth inhibitory factor （GIF）, a member of metallothionein family （metallothionein-3, MT3）, was well known by its distinct neural growth inhibitory activity, which is not shown by other MT isoforms. However, till now, people still did not know clearly how GIF exerts its biological functions. since it has been reported that GIF might serve as NO scavenger and was related to the release of zinc, our study was focused on the interaction of GIF and NO. By studying the reactions of human GIF and human MTlg with sNOC-a type of NO donor, it was found that GIF was more reactive than MT-lg toward sNOC. In order to further figure out if the high reactivity of GIF in this reaction resulted from the acid-base catalysis, several mutants were constructed： E23K, E41G/E43A, E23K/E41G/E43A. By studying their basic properties and the reactions toward sNOC, it was found that the s-nitrosylation of GIF was not only related to the acid-base catalysis, but also to the accessibility of metal-thiolate clusters.

关键词： growth inhibitory factor metallothionein s-nitrosylation acid-base catalysis

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Ghrelin-induced csrc activation through constitutive nitric oxide synthase-dependent s-nitrosylation in modulation of salivary gland acinar cell inflammatory responses to Porphyromonas gingivalis

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American Journal of Molecular Biology 2011年第2期1卷 43-51页

作者： Bronislaw L. slomiany Amalia slomiany 不详

A peptide hormone, ghrelin, recognized for its role in the regulation of nitric oxide production has emerged as an important modulator of oral mucosal inflammatory responses to periodontopathic bacterium, P. gingivalis. As csrc kinase plays a major role in controlling the activity of nitric oxide synthase (NOs) system, in this study we investigated the influence of P. gingivalis LPs on the processes of src activation in rat sublingual gland acinar cells. The LPs-induced enhancement in the activity of inducible (i) iNOs and the impairment in constitutive (c) cNOs were reflected in the suppression in csrc activity and the extent of its phosphorylation at Tyr416. Further, we show that the countering effect of ghrelin on the LPs-induced changes in csrc activity and the extent of its phosphorylation was accompanied by a marked reduction in iNOs and the increase in cNOs activation through phosphorylation at ser1179. Moreover, the effect of ghrelin on csrc activation was associated with the kinase s-nitrosylation that was susceptible to the blockage by cNOs inhibition. Our findings suggest that P. gingivalis-induced up-regulation in iNOs leads to disturbances in cNOs phosphorylation that exerts the detrimental effect on the processes of csrc activation through cNOs mediated s-nitrosylation. We also show that the effect of ghrelin on P. gingivalis-induced inflammatory changes are manifested in the enhancement in csrc activation through s-nitrosylation and the increase in its phosphorylation at Tyr416.

关键词： Ghrelin P. Gingivalis salivary Acinar Cells cNOs csrc Activation s-nitrosylation

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The interaction between Fe65 and Tip60 is regulated by s-nitrosylation on 440 cystein residue of Fe65

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Advances in Biological Chemistry 2011年第3期1卷 109-118页

作者： Eun Jeoung Lee sung Hwa shin sunghee Hyun Jaesun Chun sang sun Kang 不详

The s-nitrosylation of protein thiol groups by NO is a widely recognized protein modification. The treat-ment of cells with NOBF4 induces the s-nitrosylation of FE65. In this study, we present evidence showing that FE65 modified by NO (Nitric Oxide) via s-nitrosylation induces functional changes in the protein that inhibits the HAT activity of Tip60. The results of mutational analysis of FE65 demonstrated further that the cysteine residue of FE65 (Cys440) is critical to the process of s-nitrosylation. The mutation of the cysteine residue which completely ablated the s-nitrosylation of FE65 also lost its inhibitory effects on Tip60 HAT activity. Thus, our findings show, for the first time, that the novel regulation mechanism of Tip60 activity may operate via FE65 binding, which is enhanced by s-nitrosylation on the FE65 Cys440 residue. This study describes the interaction between FE65 and Tip60, which is enhanced by a posttransla-tional modification of FE65 (through s-nitrosylation) by NO, promoting the association of the FE65-Tip60 protein complex and inhibiting both the HAT activity of Tip60 and cell death.

关键词： s-nitrosylation NO(Nitric Oxide) FE65 HAT activity Tip60

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Modulation of gastric mucosal inflammatory responses to Helicobacter pyloriby ghrelin: Role of cNOs-dependent IKK-βs-nitrosylation in the regulation of COX-2 activation

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American Journal of Molecular Biology 2012年第2期2卷 113-123页

作者： Bronislaw L. slomiany Amalia slomiany Research Center University of Medicine and Dentistry of New Jersey Newark USA

Disturbances in nitric oxide synthase (NOs) and cyclooxygenase (COX) isozyme systems, manifested by the excessive NO and prostaglandin (PGE2) generation, are well-recognized features of gastric mucosal inflammatory responses to H. pylori infection. In this study, we report that H. pylori LPs-induced enhancement in gastric mucosal inducible (i) iNOs expression and COX-2 activation was accompanied by the impairment in constitutive (c) cNOs phosphorylation, up-regulation in the inhibitory κB kinase-β (IKKβ) activation and the increase in the transcriptional factor, NF-κB, nuclear translocation. Further, we show that abrogation of cNOs control over NF-κB activation has lead to induction of iNOs expression and COX-2 activation through s-nitrosylation. Moreover, we demonstrate that the modulatory effect of peptide hormone, ghrelin, on the LPs-induced changes was reflected in the increase in src/Akt-dependent cNOs activation through phosphorylation and the suppression of IKK-β activity through cNOs-mediated IKK-β protein s-nitrosylation. As a result, ghrelin exerted the inhibitory effect on NF-κB nuclear translocation, thus causing the repression of iNOs gene induction and the inhibition in COX-2 activation through iNOs-dependent s-nitrosylation. Our findings point to cNOs activation as a pivotal element in the signaling cascade by which ghrelin exerts modulatory control over proinflammatory events triggered in gastric mucosa by H. pylori infection.

关键词： H. pylori Gastric Mucosa iNOs Induction COX-2 Activation Ghrelin cNOs Phosphorylation IKK-β s-nitrosylation

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Cyclooxygenase-2 s-nitrosylation in salivary gland acinar cell inflammatory responses to Porphyromonas gingivalis: modulatory effect of ghrelin

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Advances in Bioscience and Biotechnology 2011年第6期2卷 434-442页

作者： Bronislaw L. slomiany Amalia slomiany 不详

Disturbances in nitric oxide synthase (NOs) system and the excessive prostaglandin (PGE2) generation are well-recognized features of oral mucosal inflammatory responses to periodontopathic bacterium, P. gingivalis. Employing rat sublingual gland acinar cells, we show that P. gingivalis LPs-induced up-regulation in PGE2 generation and the enhancement in inducible (i) iNOs activity was associated with COX-2 activation through s-nitrosylation, and accompanied by the suppression in csrc activity and the impairment in constitutive (c) cNOs phosphorylation. Further, we demonstrate that the countering effect of peptide hormone, ghrelin, on the LPs-induced changes was reflected in the increased cNOs activation through phosphorylation, repression in iNOs induction, and the reduction in PGE2 generation associated with the loss of COX-2 protein s-nitrosylation. Moreover, the effect of ghrelin on cNOs phosphorylation and the LPs-induced COX-2 s-nitrosylation was susceptible to the blockage by csrc inhibition. Our findings suggest that P. gingivalis-induced up-regulation in iNOs leads to COX-2 s-nitrosylation and up-regulation in PGE2 generation, and that the countering effect of ghrelin is mediated through src-dependent cNOs activation that is obligatory for the maintenance of iNOs gene suppression.

关键词： salivary Gland P. gingivalis iNOs Induction COX-2 Activation s-nitrosylation Ghrelin cNOs Phosphorylation

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Role of constitutive nitric oxide synthase in regulation of Helicobacter pylori-induced gastric mucosal cyclooxygenase-2 ac-tivation through s-nitrosylation: mechanism of ghrelin action

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Open Journal of Gastroenterology 2011年第2期1卷 13-22页

作者： Bronislaw L. slomiany Amalia slomiany 不详

Gastric mucosal inflammatory responses to H. pylori lipopolysaccharide (LPs), are characterized by the excessive NO and prostaglandin (PGE2) generation due to the disturbances in nitric oxide synthase (NOs) and cyclooxygenase (COX) systems. Here, we report that the LPs-induced enhancement in gastric mucosal inducible (i) iNOs) activity and up-regulation in PGE2 production was associated with the suppression in Akt kinase activity and the impairment in constitutive (c) cNOs activation. The stimulatory effect of the LPs on PGE2 production, furthermore, was susceptible to suppression by COX-2 inhibitor, Ns-398, and iNOs inhibitor, 1400 W. Further, we show that the countering effect of peptide hormone, ghrelin, on the LPs-induced changes was reflected in up-regu- lation in Akt activity and the increase in cNOs activation through phosphorylation, and accompanied by the suppression in iNOs expression and the reduction in COX-2 activity associated with the loss in COX-2 protein s-nitrosylation. Moreover, the effect of ghre-lin on the LPs-induced COX-2 s-nitrosylation was subject to repression by Akt inhibition. Our findings demonstrate that induction in iNOs with H. pylori in- fection leads to COX-2 activation through s-nitro- sylation and up-regulation in PGE2 generation, and that ghrelin counters these untoward consequences of the LPs through Akt-mediated up-regulation in cNO- s activation required for the iNOs gene repression.

关键词： H. pylori Gastric Mucosa iNOs Induction COX-2 Activation s-nitrosylation Ghrelin

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Cytosolic phospholipase A2 s-nitrosylation in ghrelin protection against detrimental effect of ethanol cytotoxicity on gastric mucin synthesis ——Ghrelin in gastric mucosal protection

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Health 2010年第9期2卷 1033-1039页

作者： Bronislaw L. slomiany Amalia slomiany 不详

Ghrelin, a peptide hormone produced mainly in the stomach, has emerged recently as an important regulator of nitric oxide synthase (NOs) and cyclooxygenase (COX) enzyme systems, the products of which play direct cytoprotective function in the maintenance of gastric mucosal integrity. In this study, using gastric mucosal cells, we report on the role of ghrelin in countering the cytotoxic effect of ethanol on mucin synthesis. We show that the countering effect of ghrelin on mucin synthesis was associated with the increase in NO and PGE2 production, and characterized by a marked up-regulation in cytosolic phospholipase A2 (cPLA2) activity. The ghrelin-induced up-regulation in mucin synthesis, like that of cPLA2 activity, was subject to suppression by src inhibitor, PP2 and ERK inhibitor, PD98059, as well as ascorbate. Moreover, the loss in countering effect of ghrelin on the ethanol cytotoxicity and mucin synthesis was attained with cNOs inhibitor, L-NAME as well as COX-1 inhibitor sC-560. The effect of L-NAME was reflected in the inhibition of ghrelin-induced mucosal cell capacity for NO production, cPLA2 s-nitrosylation and PGE2 generation, whereas COX-1 inhibitor caused only the inhibition in PGE2 generation. Our findings suggest that the activation of gastric mucosal cPLA2 through cNOs-induced s-nitrosylation plays an essential role in the countering effect of ghrelin on the disturbances in gastric mucin synthesis caused by ethanol cytotoxicity.

关键词： Ghrelin Ethanol Cytotoxicity Gastric Mucin CNOs CPLA2 s-nitrosylation

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Role of ghrelin in modulation of s-nitrosylation-Dependent akt inactivation induced in salivary gland acinar cells by porphyromonas gingivalis

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Health 2010年第12期2卷 1448-1455页

作者： Bronislaw L. slomiany Amalia slomiany 不详

Ghrelin, a peptide hormone, newly identified in oral mucosal tissue, has emerged re-cently as a principal modulator of the in-flammatory responses to bacterial infection through the regulation of nitric oxide syn-thase system. In this study, using rat sub-lingual salivary gland acinar cells, we report that lipopolysaccharide (LPs) of periodon-topathic bacterium, P. gingivalis- induced enhancement in the activity of inducible ni-tric oxide synthase (iNOs) was associated with the suppression in Akt kinase activity and the impairment in constitutive (c) cNOs phosphorylation. Further, we show that the detrimental effect of the LPs on Akt activa-tion, manifested in the kinase protein s-nitrosylation and a decrease in its phos-phorylation at ser473, was susceptible to suppression by iNOs inhibitor, 1400W. Moreover, we demonstrate that a peptide hormone, ghrelin, countered the LPs- induced changes in Akt activity and NOs system. This effect of ghrelin was reflected in the decreased in Akt s-nitrosylation and the increase in its phosphorylation at ser473, as well as cNOs activation through phos-phorylation. Our findings suggest that P. gingivalis-induced up-regulation in iNOs leads to Akt kinase inactivation through s-nitrosylation that impacts cNOs activation through phosphorylation. We also show that the countering effect of ghrelin on P. gingivalis-induced disturbances in Akt ac-tivation are manifested in a decrease in the kinase s-nitrosylation and the increase in its phosphorylation.

关键词： P. Gingivalis salivary Gland Inos Akt s-nitrosylation Cno s Phosphorylation Ghrelin

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Car-Parinello molecular dynamics simulations of thionitroxide and s-nitrosothiol in the gas phase,methanol,and water——A theoretical study of s-nitrosylation

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中国科学:化学 2012年第10期42卷 1497-1498页

作者： LIANG Juan1,CHENG shangLi1,HOU JunWei1,XU ZhenHao1,2 & ZHAO Yi-Lei1,2,3* 1 state Key Laboratory of Microbial Metabolism,school of Life sciences and Biotechnology,shanghai Jiao Tong University,shanghai 200240,China 2 shanghai Center for systems Biomedicine,shanghai Jiao Tong University,shanghai 200240,China 3 MOE Laboratory of scientific and Engineering Computing,shanghai Jiao Tong University,shanghai 200240,China state Key Laboratory of Microbial Metabolism school of Life sciences and Biotechnology shanghai Jiao Tong University shanghai 200240 China shanghai Center for systems Biomedicine shanghai Jiao Tong University shanghai 200240 China MOE Laboratory of scientific and Engineering Computing shanghai Jiao Tong University shanghai 200240 China

A dilemma about whether thionitroxide radical(RsNHO) or s-nitrosothiol(RsNO) is observed in protein s-nitrosylation has arisen recently.To illustrate the effect of chemical environment on these structures,this paper presents quantum mechanical molecular dynamics of thionitroxide,and cis-and trans-s-nitrosothiols in the gas phase,methanol,and water.By using Car-Parrinello molecular dynamics(CPMD),we have observed that there is free rotation about the s-N bond at 300 K in thionitroxide,but no such rotation is observed for s-nitrosothiol.The C-s-N-O torsion angle distribution in thionitroxide is significantly dependent upon the surrounding environment,leading to either gauche-,cis-,or trans-conformation.In the case of s-nitrosothiol the C-s-N-O plane is twisted slightly by 5°-15° in the cis-isomer,while the periplanar structure is well-retained in the trans-isomer.The calculated results are in agreement with the X-ray crystallographic data of small molecular RsNO species.Interestingly,for both compounds,the CPMD simulations show that solvation can cause a decrease in the s-N bond length.Moreover,the oxygen atom of thionitroxide is found to be a good hydrogen-bond acceptor,forming an oxyanion-hole-like hydrogen bonding network.

关键词： quantum mechanical molecular dynamics s-nitrosylation thionitroxide s-nitrosothiol solvent effect

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