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).
| Identifer | oai:union.ndltd.org:netd.ac.za/oai:union.ndltd.org:uwc/oai:etd.uwc.ac.za:11394/5206 |
| Date | January 2012 |
| Creators | Onyemata, Ezenwa James |
| Contributors | Pugh, David J.R., Atkinson, A, Rafudeen, M. S. |
| Publisher | University of the Western Cape |
| Source Sets | South African National ETD Portal |
| Language | English |
| Detected Language | English |
| Type | Thesis |
| Rights | University of the Western Cape |
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