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Structural and functional studies of XvPrx2, a type II peroxiredoxin protein from the resurrection plant xerophyta viscosa

Philosophiae Doctor - PhD / 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).

Identiferoai:union.ndltd.org:netd.ac.za/oai:union.ndltd.org:uwc/oai:etd.uwc.ac.za:11394/5206
Date January 2012
CreatorsOnyemata, Ezenwa James
ContributorsPugh, David J.R., Atkinson, A, Rafudeen, M. S.
PublisherUniversity of the Western Cape
Source SetsSouth African National ETD Portal
LanguageEnglish
Detected LanguageEnglish
TypeThesis
RightsUniversity of the Western Cape

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