Mutation of residue arginine 330 of arginine kinase results in the generation of the oxidized form more susceptible

Wang, Weidong; Shi, Yue; Zhang, Xinchao; Pan, Junhao; Zou, Guolin

doi:10.1016/j.ijbiomac.2012.12.015

Cited by 4 publications

(5 citation statements)

References 33 publications

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“…Three peptides covering C161, C222, and the active site C293 were found to be IAM labeled. The corresponding latter two cysteines form an intramolecular disulfide in Limulus arginine kinase ( 72 ). Overexpression of the enzymes confers T. brucei with increased resistance toward H 2 O 2 in accordance with a role in the oxidative stress response ( 71 ).…”

Section: Resultsmentioning

confidence: 99%

Stress-Induced ProteinS-Glutathionylation andS-Trypanothionylation in African Trypanosomes—A Quantitative Redox Proteome and Thiol Analysis

Ulrich

Finkenzeller

Merker

et al. 2017

Antioxidants & Redox Signaling

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Aims: Trypanosomatids have a unique trypanothione-based thiol redox metabolism. The parasite-specific dithiol is synthesized from glutathione and spermidine, with glutathionylspermidine as intermediate catalyzed by trypanothione synthetase. In this study, we address the oxidative stress response of African trypanosomes with special focus on putative protein S-thiolation.Results: Challenging bloodstream Trypanosoma brucei with diamide, H2O2 or hypochlorite results in distinct levels of reversible overall protein S-thiolation. Quantitative proteome analyses reveal 84 proteins oxidized in diamide-stressed parasites. Fourteen of them, including several essential thiol redox proteins and chaperones, are also enriched when glutathione/glutaredoxin serves as a reducing system indicating S-thiolation. In parasites exposed to H2O2, other sets of proteins are modified. Only three proteins are S-thiolated under all stress conditions studied in accordance with a highly specific response. H2O2 causes primarily the formation of free disulfides. In contrast, in diamide-treated cells, glutathione, glutathionylspermidine, and trypanothione are almost completely protein bound. Remarkably, the total level of trypanothione is decreased, whereas those of glutathione and glutathionylspermidine are increased, indicating partial hydrolysis of protein-bound trypanothione. Depletion of trypanothione synthetase exclusively induces protein S-glutathionylation. Total mass analyses of a recombinant peroxidase treated with T(SH)2 and either diamide or hydrogen peroxide verify protein S-trypanothionylation as stable modification.Innovation: Our data reveal for the first time that trypanosomes employ protein S-thiolation when exposed to exogenous and endogenous oxidative stresses and trypanothione, despite its dithiol character, forms protein-mixed disulfides.Conclusion: The stress-specific responses shown here emphasize protein S-trypanothionylation and S-glutathionylation as reversible protection mechanism in these parasites. Antioxid. Redox Signal. 27, 517–533.

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Section: Resultsmentioning

confidence: 99%

Stress-Induced ProteinS-Glutathionylation andS-Trypanothionylation in African Trypanosomes—A Quantitative Redox Proteome and Thiol Analysis

Ulrich

Finkenzeller

Merker

et al. 2017

Antioxidants & Redox Signaling

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“…As described by Wang et al (2013), AK contains six free cysteine thiols in its molecule, and the intramolecular disulfide bond that forms between Cys 201 and Cys 271 is essential for the structural stability of AK. Cys 271 is reported to be located in the hinge region between the two domains of AK and causes conformational changes in the enzyme when the substrate is added (Liu et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Mapping and characterization of antigenic epitopes of arginine kinase of Scylla paramamosain

Yang

Cao

Alcocer

et al. 2015

Molecular Immunology

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“…The amino-acid residues CPTNLGT located at C-terminus formed a functional domain (Uda & Suzuki, 2004). The C270 was demonstrated to be involved in holding AK activity and constraining the orientation of the substrate arginine (Guo et al , 2004), while L112, T272, and R329 played key roles in AK activity, substrate synergism, and structural stability, respectively (Li et al , 2013; Wang et al , 2013; Wu et al , 2014). The HaAK expression analysis indicated that it may participate in the process of larval development.…”

Section: Discussionmentioning

confidence: 99%

The effect of silencing arginine kinase by RNAi on the larval development of Helicoverpa armigera

et al. 2015

Bull. Entomol. Res.

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Arginine kinase (AK) is an important regulation factor of energy metabolism in invertebrate. An arginine kinase gene, named HaAK, was identified to be differentially expressed between Cry1Ac-susceptible (96S) and Cry1Ac-resistant (Bt-R) Helicoverpa armigera larvae using cDNA-amplification fragment length polymorphism analysis. The full-length open reading frame sequence of HaAK gene with 1068 bp was isolated from H. armigera. Quantitative reverse transcription polymerase chain reaction assay revealed that HaAK gene is specifically expressed in multiple tissues and at larval developmental stages. The peak expression level of HaAK was detected in the midgut of the fifth-instar larvae. Moreover, the expression of HaAK was obviously down-regulated in Bt-R larvae. We further constructed a dsRNA vector directly targeting HaAK and employed RNAi technology to control the larvae. The feeding bioassays showed that minute quantities of dsRNA could greatly increase the larval mortality and delay the larval pupation. Silencing of HaAK significantly retarded the larval development, indicating that HaAK is a potential target for RNA interference-based pest management.

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Mutation of residue arginine 330 of arginine kinase results in the generation of the oxidized form more susceptible

Cited by 4 publications

References 33 publications

Stress-Induced ProteinS-Glutathionylation andS-Trypanothionylation in African Trypanosomes—A Quantitative Redox Proteome and Thiol Analysis

Stress-Induced ProteinS-Glutathionylation andS-Trypanothionylation in African Trypanosomes—A Quantitative Redox Proteome and Thiol Analysis

Mapping and characterization of antigenic epitopes of arginine kinase of Scylla paramamosain

The effect of silencing arginine kinase by RNAi on the larval development of Helicoverpa armigera

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