Molecular and biochemical characterisation of a novel type II peroxiredoxin (XvPrx2) from the resurrection plant Xerophyta viscosa
Kershini Govender A , Jennifer A. Thomson A , Sagadevan Mundree B , Abdelaleim Ismail ElSayed C and Mohammed Suhail Rafudeen A D
+ Author Affiliations
- Author Affiliations
A Department of Molecular and Cell Biology, University of Cape Town, Private Bag, Rondebosch, 7701, South Africa.
B Centre for Tropical Crops and Biocommodities, Queensland University of Technology, PO Box 2434, Brisbane, Qld 4001, Australia.
C Biochemistry Department, Faculty of Agriculture, Zagazig University, 44 519 Zagazig, Egypt.
D Corresponding author. Email: suhail.rafudeen@uct.ac.za
Functional Plant Biology 43(7) 669-683 https://doi.org/10.1071/FP15291
Submitted: 28 September 2015 Accepted: 27 November 2015 Published: 12 January 2016
Abstract
A type II peroxiredoxin gene (XvPrx2) was isolated from a Xerophyta viscosa (Baker) cDNA cold-stress library. The polypeptide displayed significant similarity to other plant type II peroxiredoxins, with the conserved amino acid motif (PGAFTPTCS) proposed to constitute the active site of the enzyme. Northern blot analyses showed that XvPrx2 gene was stress-inducible in response to abiotic stresses while gel analyses revealed that XvPrx2 homologues exist within the X. viscosa proteome. Using a yellow fluorescent reporter protein, the XvPrx2 protein localised to the cytosol. A mutated protein (XvV7) was generated by converting the valine at position 76 to a cysteine and an in vitro DNA protection assay showed that, in the presence of either XvPrx2 or XvV7, DNA protection occurred. In addition, an in vivo assay showed that increased protection was conferred to Escherichia coli cells overexpressing either XvPrx2 or XvV7. The XvPrx2 activity was maximal with DTT as electron donor and H2O2 as substrate. Using E. coli thioredoxin, a 2–15-fold lower enzyme activity was observed. The XvPrx2 activity with glutathione was significantly lower and glutaredoxin had no measurable effect on this reaction. The XvV7 protein displayed significantly lower activity compared with XvPrx2 for all substrates assessed.
Additional keywords: desiccation tolerance, free radicals, peroxiredoxin, resurrection plant.
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