The Arabidopsis DJ-1a protein confers stress protection through cytosolic SOD activationVisa övriga samt affilieringar
2010 (Engelska)Ingår i: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 123, nr 10, s. 1644-1651Artikel i tidskrift (Refereegranskat) Published
Abstract [en]
Mutations in the DJ-1 gene (also known as PARK7) cause inherited Parkinson's disease, which is characterized by neuronal death. Although DJ-1 is thought to be an antioxidant protein, the underlying mechanism by which loss of DJ-1 function contributes to cell death is unclear. Human DJ-1 and its Arabidopsis thaliana homologue, AtDJ-1a, are evolutionarily conserved proteins, indicating a universal function. To gain further knowledge of the molecular features associated with DJ-1 dysfunction, we have characterized AtDJ-1a. We show that AtDJ-1a levels are responsive to stress treatment and that AtDJ-1a loss of function results in accelerated cell death in aging plants. By contrast, transgenic plants with elevated AtDJ-1a levels have increased protection against environmental stress conditions, such as strong light, H2O2, methyl viologen and copper sulfate. We further identify superoxide dismutase 1 (SOD1) and glutathione peroxidase 2 (GPX2) as interaction partners of both AtDJ-1a and human DJ-1, and show that this interaction results in AtDJ-1a- and DJ-1-mediated cytosolic SOD1 activation in a copper-dependent fashion. Our data have highlighted a conserved molecular mechanism for DJ-1 and revealed a new protein player in the oxidative stress response of plants.
Ort, förlag, år, upplaga, sidor
The Company of Biologists , 2010. Vol. 123, nr 10, s. 1644-1651
Nyckelord [en]
Arabidopsis, Stress, DJ-1
Nationell ämneskategori
Cellbiologi Cell- och molekylärbiologi
Identifikatorer
URN: urn:nbn:se:umu:diva-188654DOI: 10.1242/jcs.063222ISI: 000277357400005PubMedID: 20406884Scopus ID: 2-s2.0-77952353245OAI: oai:DiVA.org:umu-188654DiVA, id: diva2:1603814
2021-10-182021-10-182021-10-18Bibliografiskt granskad