Characterization of a bacterioferritin comigratory protein family 1-Cys peroxiredoxin from Candidatus Liberibacter asiaticus
| Autor: | Ashwani Sharma, Prabhat Pratap Singh Tomar, Sumit Bhose, Dilip Kumar Ghosh, Partha Pratim Roy, Narender Kumar, Anamika Singh |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Antioxidant Protein family Cell Survival medicine.medical_treatment Apoptosis Plant Science medicine.disease_cause 03 medical and health sciences Bacterial Proteins Rhizobiaceae Chlorocebus aethiops medicine Animals Humans Amino Acid Sequence 030102 biochemistry & molecular biology biology food and beverages Cell Biology General Medicine Bacterioferritin Free Radical Scavengers Hydrogen Peroxide Peroxiredoxins Cytochrome b Group Oxidative Stress 030104 developmental biology Cell killing Biochemistry COS Cells Ferritins biology.protein MCF-7 Cells Peroxiredoxin Oxidation-Reduction Oxidative stress Peroxidase Cysteine |
| Zdroj: | Protoplasma. 254(4) |
| ISSN: | 1615-6102 |
| Popis: | To defend against the lethality of the reactive oxygen species (ROS), nature has armed microorganisms with a range of antioxidant proteins. These include peroxiredoxin (Prx) super family proteins which are ubiquitous cysteine-based non-heme peroxidases. The phytopathogenic bacterium Candidatus Liberibacter asiaticus (CLA), an etiological agent of citrus plants diseases, posses many genes for defense against oxidative stress. The bacterioferritin comigratory protein (BCP), a member of Prxs, is part of an oxidative stress defense system of CLA. The key residue of these enzymes is peroxidatic Cys (termed CPSH) which is contained within an absolutely conserved PXXX (T/S) XXC motif. In the present study, a 1-Cys Prx enzyme (CLa-BCP), having CPSH/sulfenic acid cysteine (C-46) but lacking the resolving cysteine (CRSH), was characterized from CLA. The peroxidase activity was demonstrated using a non-physiological electron donor DTT against varied substrates. The protein was shown to have the defensive role against peroxide-mediated cell killing and an antioxidant activity. In vitro DNA-binding studies showed that this protein can protect supercoiled DNA from oxidative damage. To the best of our knowledge, this is the first report on a 1-Cys BCPs to have an intracellular reactive oxygen species scavenging activity. |
| Databáze: | OpenAIRE |
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