A novel stress-inducible antioxidant enzyme identified from the resurrection plant Xerophyta viscosa Baker.
A cDNA corresponding to 1-Cys peroxiredoxin, an evolutionarily conserved thiol-specific antioxidant enzyme, was isolated from Xerophyta viscosa Baker, a resurrection plant indigenous to Southern Africa and belonging to the family Velloziaceae. The cDNA, designated XvPer1, contains an open reading frame that encodes a polypeptide of 219 residues with a predicted molecular weight of 24.2 kDa. The XvPer1 polypeptide shows significant sequence identity (approx. 70%) to other recently identified plant 1-Cys peroxiredoxins and relatively high levels of sequence similarity (approx. 40%) to non-plant 1-Cys peroxiredoxins. The XvPer1 cDNA contains a putative polyadenylation site. As for all 1-Cys peroxiredoxins identified to date, the amino acid sequence proposed to constitute the active site of the enzyme, PVCTTE, is highly conserved in XvPer1. It also contains a putative bipartite nuclear localization signal. Southern blot analysis revealed that there is a single copy of XvPer1 in the X. viscosa genome. All angiosperm 1-Cys peroxiredoxins described to date are seed-specific and absent in vegetative tissues even under stress conditions; therefore, XvPer1 is unique in that it is expressed in the vegetative tissues of X. viscosa. The XvPer1 transcript was absent in fully hydrated X. viscosa tissue but levels increased in tissues subjected to abiotic stresses such as dehydration, heat (42 degrees C), high light intensity (1,500 micro mol photons m(-2) s(-1)) and when treated with abscisic acid (100 micro M ABA) and sodium chloride (100 mM NaCl). Western blot analyses correlated with the patterns of expression of XvPer1 transcripts under different stress conditions. Immunofluorescence analyses revealed that XvPer1 is localized in the nucleus of dehydrated X. viscosa leaf cells. These results suggest that XvPer1 is a stress-inducible gene, which may function to protect nucleic acids within the nucleus against oxidative injury.
Mowla
Shaheen B
SB
Department of Molecular and Cell Biology, University of Cape Town, Private Bag, Rondebosch, 7701, South Africa.
Thomson
Jennifer A
JA
Farrant
Jill M
JM
Mundree
Sagadevan G
SG
D000040:Abscisic Acid / Q000494:pharmacology; D000595:Amino Acid Sequence; D000975:Antioxidants / Q000302:isolation & purification / Q000378:metabolism*; D001483:Base Sequence; D015153:Blotting, Western; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D015971:Gene Expression Regulation, Enzymologic / Q000187:drug effects; D018506:Gene Expression Regulation, Plant / Q000187:drug effects; D006358:Hot Temperature; D008027:Light; D019684:Magnoliopsida / Q000201:enzymology* / Q000235:genetics; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D018384:Oxidative Stress / Q000502:physiology*; D010544:Peroxidases / Q000235:genetics* / Q000378:metabolism; D054464:Peroxiredoxins; D010802:Phylogeny; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D012965:Sodium Chloride / Q000494:pharmacology
D000975:Antioxidants; D018076:DNA, Complementary; D010940:Plant Proteins; D012965:Sodium Chloride; D000040:Abscisic Acid; D010544:Peroxidases; D054464:Peroxiredoxins