共查询到20条相似文献,搜索用时 15 毫秒
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Many TFIIIA‐type zinc finger proteins (ZFPs) play important roles in stress responses in plants. In the present study, a novel zinc finger protein gene, StZFP1, was cloned from potato. StZFP1 is a typical TFIIIA‐type two‐finger zinc finger gene with one B‐box domain, one L‐box domain and a DLN‐box/EAR motif. The StZFP1 genes belong to a small gene family with an estimated copy number of four or five, located on chromosome I. StZFP1 is constitutively expressed in leaves, stems, roots, tubers and flowers of adult plants. Expression of StZFP1 can be induced by salt, dehydration and exogenously applied ABA. StZFP1 expression is also responsive to infection by the late blight pathogen Phytophthora infestans. Transient expression analysis of StZFP1:GFP fusion protein revealed that StZFP1 is preferentially localised in the nucleus. Ectopic expression of StZFP1, driven by the Arabidopsis rd29A promoter in transgenic tobacco, increased plant tolerance to salt stress. These results demonstrate that StZFP1 might be involved in potato responses to salt and dehydration stresses through an ABA‐dependent pathway. 相似文献
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Sargisova YG Andreasyan NA Hayrapetyan HL Harutyunyan HA 《Biochemistry. Biokhimii?a》2012,77(1):92-97
In this study we have investigated the effect of reactive oxygen species produced by some chemicals in aqueous solutions on
activity of adenosine deaminase 2 (ADA2) purified from human blood plasma. An activating effect on ADA2 was observed in vitro with sodium nitroprusside (SNP), the source of NO (nitrosonium ions NO− in aqueous solutions). Not SH-groups of cysteine but other amino acid residues sensitive to NO were responsible for ADA2
activation. The SNP-derived activation was more pronounced when purified ADA2 was preincubated with heparin and different
proteins as an experimental model of the protein environment in vivo. The most effective was heparin, which is known for its ability to regulate enzyme and protein functions in extracellular
matrix. We conclude that ADA2 is a protein with flexible conformation that is affected by the protein environment, and it
changes its activity under oxidative (nitrosative) stress. 相似文献
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Nitric oxide (NO), a gaseous free radical that is synthesized in organisms by nitric oxide synthases, participates in a critical
fashion in the regulation of diverse physiological functions such as vascular and neuronal signal transduction, host defense,
and cell death regulation. Two major pathways of NO signaling involve production of the second messenger guanosine 3′,5′-cyclic
monophosphate (cGMP) and posttranslational modification (PTM) of redox-sensitive cysteine thiols of proteins. We recently
clarified the physiological formation of 8-nitroguanosine 3′,5′-cyclic monophosphate (8-nitro-cGMP) as the first demonstration,
since the discovery of cGMP more than 40 years ago, of a new second messenger derived from cGMP in mammals. 8-Nitro-cGMP is
electrophilic and reacts efficiently with sulfhydryls of proteins to produce a novel PTM via cGMP adduction, a process that
we named protein S-guanylation. 8-Nitro-cGMP may regulate electrophilic signaling on the basis of its electrophilicity through induction of
S-guanylation of redox sensor proteins. Examples include S-guanylation of the redox sensor protein Kelch-like ECH-associated protein 1 (Keap1), which leads to activation of NF-E2-related
factor 2 (Nrf2)-dependent expression of antioxidant and cytoprotective genes. This S-guanylation-mediated activation of an antioxidant adaptive response may play an important role in cytoprotection during bacterial
infections and oxidative stress. Identification of new redox-sensitive proteins as targets for S-guanylation may help development of novel therapeutics for oxidative stress- and inflammation-related disorders and vascular
diseases as well as understanding of cellular protection against oxidative stress. 相似文献
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Bret D. Wallace R. Scott Williams 《Protein science : a publication of the Protein Society》2016,25(9):1682-1691
Cells use the post‐translational modification ADP‐ribosylation to control a host of biological activities. In some pathogenic bacteria, an operon‐encoded mono‐ADP‐ribosylation cycle mediates response to host‐induced oxidative stress. In this system, reversible mono ADP‐ribosylation of a lipoylated target protein represses oxidative stress response. An NAD+‐dependent sirtuin catalyzes the single ADP‐ribose (ADPr) addition, while a linked macrodomain‐containing protein removes the ADPr. Here we report the crystal structure of the sitruin‐linked macrodomain protein from Staphylococcus aureus, SauMacro (also known as SAV0325) to 1.75‐Å resolution. The monomeric SauMacro bears a previously unidentified Zn2+‐binding site that putatively aids in substrate recognition and catalysis. An amino‐terminal three‐helix bundle motif unique to this class of macrodomain proteins provides a structural scaffold for the Zn2+ site. Structural features of the enzyme further indicate a cleft proximal to the Zn2+ binding site appears well suited for ADPr binding, while a deep hydrophobic channel in the protein core is suitable for binding the lipoate of the lipoylated protein target. 相似文献
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Barbara De Smet Patrick Willems Alvaro D. Fernandez‐Fernandez Saleh Alseekh Alisdair R. Fernie Joris Messens Frank Van Breusegem 《The Plant journal : for cell and molecular biology》2019,97(4):765-778
Protein cysteine thiols are post‐translationally modified under oxidative stress conditions. Illuminated chloroplasts are one of the important sources of hydrogen peroxide (H2O2) and are highly sensitive to environmental stimuli, yet a comprehensive view of the oxidation‐sensitive chloroplast proteome is still missing. By targeting the sulfenic acid YAP1C‐trapping technology to the plastids of light‐grown Arabidopsis cells, we identified 132 putatively sulfenylated plastid proteins upon H2O2 pulse treatment. Almost half of the sulfenylated proteins are enzymes of the amino acid metabolism. Using metabolomics, we observed a reversible decrease in the levels of the amino acids Ala, Asn, Cys, Gln, Glu, His, Ile, Leu, Lys, Phe, Ser, Thr and Val after H2O2 treatment, which is in line with an anticipated decrease in the levels of the glycolysis and tricarboxylic acid metabolites. Through the identification of an organelle‐tailored proteome, we demonstrated that the subcellular targeting of the YAP1C probe enables us to study in vivo cysteine sulfenylation at the organellar level. All in all, the identification of these oxidation events in plastids revealed that several enzymes of the amino acid metabolism rapidly undergo cysteine oxidation upon oxidative stress. 相似文献
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Regulation,sensory domains and roles of two Desulfovibrio desulfuricans ATCC27774 Crp family transcription factors,HcpR1 and HcpR2, in response to nitrosative stress
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Ian T. Cadby Susan A. Ibrahim Matthew Faulkner David J. Lee Douglas Browning Stephen J. Busby Andrew L. Lovering Melanie R. Stapleton Jeffrey Green Jeffrey A. Cole 《Molecular microbiology》2016,102(6):1120-1137
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Concomitant production of nitric oxide and superoxide in biological systems has been proposed to generate numerous reactive oxygen and nitrogen species that cause oxidative and nitrosative stress. Thiols, especially glutathione, play an important role in cellular defense against radical species. In the present study, we investigated and compared the anti-nitrosative activity of a wide range of thiols in a simplified chemical system of co-generated nitric oxide and superoxide. Of the 13 thiols studied, three groups of thiols are distinguishable: (i) Group I includes cysteine and its four congeners (cysteine methyl ester, cysteine ethyl ester, homocysteine, cysteamine); they are subject to rapid oxidative decomposition and have the least anti-nitrosative activity. (ii) Group II consists of glutathione, penicillamine, tiopronin and mesna; they have the greatest effect on delaying the nitrosation reaction. (iii) Group III comprises N-acetylcysteine, N-acetylpenicillamine, captopril, and thioglycolate; they all have high pKa for the mercapto group and show the strongest inhibitory effect on the rate and extent of nitrosation in the system studied. 相似文献
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Lili Wang Changchun Yu Shanglin Xu Yingguo Zhu Wenchao Huang 《Plant, cell & environment》2016,39(12):2740-2753
The drought‐induced 19 protein family consists of several atypical Cys2/His2‐type zinc finger proteins in plants and plays an important role in abiotic stress. In this study, we found that overexpressing OsDi19‐4 in rice altered the expression of a series of abscisic acid (ABA)‐responsive genes, resulting in strong ABA‐hypersensitive phenotypes including ABA‐induced seed germination inhibition, early seedling growth inhibition and stomatal closure. On the contrary, OsDi19‐4 knockdown lines were less sensitive to ABA. Additionally, OsCDPK14 was identified to interact with OsDi19‐4 and be responsible for the phosphorylation of OsDi19‐4, and the phosphorylation of OsDi19‐4 was further enhanced after the treatment of ABA. Apart from these, OsDi19‐4 was shown to directly bind to the promoters of OsASPG1 and OsNAC18 genes, two ABA‐responsive genes, and regulate their expression. Transient expression assays confirmed the direct regulation role of OsDi19‐4, and the regulation was further enhanced by the increased phosphorylation of OsDi19‐4 after the treatment of ABA. Taken together, these data demonstrate that OsDi19‐4 acts downstream of OsCDPK14 to positively regulate ABA response by modulating the expression of ABA‐responsive genes in rice. 相似文献