Structural and functional studies of XvPrx2, a type II peroxiredoxin protein from the resurrection plant xerophyta viscosa
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Date
2012
Authors
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Publisher
University of the Western Cape
Abstract
XvPrx2 is a 1-Cys-containing member of the Prx5 subfamily of peroxiredoxins isolated
from the resurrection plant Xerophyta viscosa. It is reported to be up-regulated during
periods of desiccation and to protect nucleic acids and cellular proteins from oxidative
damage through scavenging of reactive oxygen species, suggesting that it may play a
role the desiccation tolerance of X. viscosa (Govender, 2006). Members of the Prx5
subfamily have previously been reported to occur as non-covalent homodimers
associating across an A-type interface. PrxD from Populus tremula, a close homologue
of XvPrx2, forms disulphide bonds with glutathione (glutathionylation) resulting in the
unfolding of the Cp-loop and α2-helix and disruption of the homodimer, on the basis of
which glutathionylation has been proposed as a physiological mechanism for
regeneration of all members of the Prx5 subfamily (Noguera-Mazon, et al., 2006b).
Description
Philosophiae Doctor - PhD
Keywords
Peroxiredoxin protein, Resurrection plant, Xerophyta viscosa