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

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dc.contributor.advisorPugh, David J.R.
dc.contributor.advisorAtkinson, A
dc.contributor.advisorRafudeen, M. S.
dc.contributor.authorOnyemata, Ezenwa James
dc.date.accessioned2016-08-23T10:52:01Z
dc.date.accessioned2024-05-09T08:19:21Z
dc.date.available2016-08-23T10:52:01Z
dc.date.available2024-05-09T08:19:21Z
dc.date.issued2012
dc.descriptionPhilosophiae Doctor - PhDen_US
dc.description.abstractXvPrx2 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).en_US
dc.identifier.urihttps://hdl.handle.net/10566/13530
dc.language.isoenen_US
dc.publisherUniversity of the Western Capeen_US
dc.rights.holderUniversity of the Western Capeen_US
dc.subjectPeroxiredoxin proteinen_US
dc.subjectResurrection planten_US
dc.subjectXerophyta viscosaen_US
dc.titleStructural and functional studies of XvPrx2, a type II peroxiredoxin protein from the resurrection plant xerophyta viscosaen_US
dc.typeThesisen_US

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Philosophiae Doctor - PhD (Biotechnology)