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 |
Page generated in 0.0014 seconds