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PMID:27987036
Citation |
'Singh, A, Kumar, N, Tomar, PP, Bhose, S, Ghosh, DK, Roy, P and Sharma, AK (2016) Characterization of a bacterioferritin comigratory protein family 1-Cys peroxiredoxin from Candidatus Liberibacter asiaticus. Protoplasma ' |
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Abstract |
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. |
Links |
PubMed Online version:10.1007/s00709-016-1062-z |
Keywords |
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Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|
GO:0051920: peroxiredoxin activity |
ECO:0000314: |
F |
Figure 3, part a, shows the peroxiredoxin assay and the significance of CLa-BCP in removing H2O2. There is an indirect relationship between the amount of Cla-BCP and the percentage of disappearance of H2O2 Liberibacter asiaticus" (aka Candidatus Liberibacter asiaticus psy62) |
complete | ||||
GO:0042262: DNA protection |
ECO:0000314: |
P |
Figure 8a shows the clear protective nature of CLa-BCP on coiled DNA. Lane 1 was the control group for demonstrating protected (coiled) DNA. Lanes 3 and 4 which contained CLa-BCP show nicked circular (NC) DNA and supercoiled (SC) DNA rather than in lane 2 which showed uncoiled, unprotected, linear DNA from the effects of H2O2. "The BCP gene (GenBank: ACT56685.1, originally annotated as BCP gene) was amplified by PCR using CLA genomic DNA." This corresponds to CLIBASIA_00485. |
complete | ||||
GO:0051920: peroxiredoxin activity |
ECO:0000247: |
UniProtKB:Q9ZMU4
|
F |
Candidatus LIberibacter aciaticus, Cla Bacterioferritin comigratory protein, BCP In figure 1 they did a sequence alignment for Cla-BCP with Helicobacter pylori strain J99. |
complete | |||
GO:0051920: peroxiredoxin activity |
ECO:0000247: |
UniProtKB:Q8YC48
|
F |
Candidatus LIberibacter aciaticus, CLa Bacterioferritin comigratory protein, BCP In figure 1 they did a sequence alignment for Cla-BCP with Brucella melitensis strain 16M. |
complete | |||
GO:0042964: thioredoxin reduction |
ECO:0000314: |
P |
Thioredoxin activity also observed in PMID:20335172[1], their results were not shown in that experiment but were mentioned. |
complete | ||||
Notes
See also
References
See Help:References for how to manage references in GONUTS.
- ↑ Horta, BB et al. (2010) Structural and biochemical characterization of peroxiredoxin Qbeta from Xylella fastidiosa: catalytic mechanism and high reactivity. J. Biol. Chem. 285 16051-65 PubMed GONUTS page