Peer-Reviewed Journal Details
Mandatory Fields
Culleton, BA;Lall, P;Kinsella, GK;Doyle, S;McCaffrey, J;Fitzpatrick, DA;Burnell, AM
2015
January
Cell Stress and Chaperones
A role for the Parkinson's disease protein DJ-1 as a chaperone and antioxidant in the anhydrobiotic nematode Panagrolaimus superbus
Published
4 ()
Optional Fields
RESOLUTION CRYSTAL-STRUCTURE ESCHERICHIA-COLI HSP31 DESICCATION-TOLERANCE MOLECULAR-DYNAMICS OXIDATIVE STRESS INTRACELLULAR PROTEASE PROKARYOTIC HOMOLOG ALPHA-SYNUCLEIN WATER-STRESS LEA PROTEINS
20
121
137
Mutations in the human DJ-1/PARK7 gene are associated with familial Parkinson's disease. DJ-1 belongs to a large, functionally diverse family with homologues in all biological kingdoms. Several activities have been demonstrated for DJ-1: an antioxidant protein, a redox-regulated molecular chaperone and a modulator of multiple cellular signalling pathways. The majority of functional studies have focussed on human DJ-1 (hDJ-1), but studies on DJ-1 homologues in Drosophila melanogaster, Caenorhabditis elegans, Dugesia japonica and Escherichia coli also provide evidence of a role for DJ-1 as an antioxidant. Here, we show that dehydration is a potent inducer of a dj-1 gene in the anhydrobiotic nematode Panagrolaimus superbus. Our secondary structure and homology modelling analyses shows that recombinant DJ-1 protein from P. superbus (PsuDJ-1.1) is a well-folded protein, which is similar in structure to the hDJ-1. PsuDJ-1.1 is a heat stable protein; with T-1/2 unfolding transition values of 76 and 70 A degrees C obtained from both circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) measurements respectively. We found that PsuDJ-1.1 is an efficient antioxidant that also functions as a 'holdase' molecular chaperone that can maintain its chaperone function in a reducing environment. In addition to its chaperone activity, PsuDJ-1.1 may also be an important non-enzymatic antioxidant, capable of providing protection to P. superbus from oxidative damage when the nematodes are in a desiccated, anhydrobiotic state.
DORDRECHT
1355-8145
10.1007/s12192-014-0531-6
Grant Details