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CENTRIN2 Interacts with the Arabidopsis Homolog of the Human XPC Protein (AtRAD4) and Contributes to Efficient Synthesis-dependent Repair of Bulky DNA Lesions

Liang, Lu ; Flury, Sabine ; Kalck, Véronique ; Hohn, Barbara ; Molinier, Jean

In: Plant Molecular Biology, 2006, vol. 61, no. 1-2, p. 345-356

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    Titre
    • CENTRIN2 Interacts with the Arabidopsis Homolog of the Human XPC Protein (AtRAD4) and Contributes to Efficient Synthesis-dependent Repair of Bulky DNA Lesions
    Auteur
    • Liang, Lu. Plant Biochemistry Physiology Group, Federal Institute of Technology (ETH) Zurich, Institute of Plant Sciences, Experimental Station Eschikon 33, CH-8315, Lindau, Switzerland
    • Flury, Sabine. Swiss Federal Institute for Environmental Science & Technology (EAWAG), Limnogical Research, Ueberlandstrasse 133, CH-8600, Duebendorf, Switzerland
    • Kalck, Véronique. Friedrich Miescher Institute, Maulbeerstrasse 66, CH 4058, Basel, Switzerland
    • Hohn, Barbara. Friedrich Miescher Institute, Maulbeerstrasse 66, CH 4058, Basel, Switzerland
    • Molinier, Jean. Friedrich Miescher Institute, Maulbeerstrasse 66, CH 4058, Basel, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Plant Molecular Biology, 2006, vol. 61, no. 1-2, p. 345-356. Kluwer Academic Publishers
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:317414
    Summary
    Arabidopsis thaliana CENTRIN2 (AtCEN2) has been shown to modulate Nucleotide Excision Repair (NER) and Homologous Recombination (HR). The present study provides evidence that AtCEN2 interacts with the Arabidopsis homolog of human XPC, AtRAD4 and that the distal EF-hand Ca2+ binding domain is essential for this interaction. In addition, the synthesis-dependent repair efficiency of bulky DNA lesions was enhanced in cell extracts prepared from Arabidopsis plants overexpressing the full length AtCEN2 but not in those overexpressing a truncated AtCEN2 form, suggesting a role for the distal EF-hand Ca2+ binding domain in the early step of the NER process. Upon UV-C treatment the AtCEN2 protein was shown to be increased in concentration and to be localised in the nucleus rapidly. Taken together these data suggest that AtCEN2 is a part of the AtRAD4 recognition complex and that this interaction is required for efficient NER. In addition, NER and HR appear to be differentially modulated upon exposure of plants to DNA damaging agents. This suggests in plants, that processing of bulky DNA lesions highly depends on the excision repair efficiency, especially the recognition step, thus influencing the recombinational repair pathway