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DNA-binding activity of the N-terminal cleavage product of poly(ADP-ribose) polymerase is required for UV mediated apoptosis.

Authors
Kim, JW; Won, J; Sohn, S; Joe, CO
Citation
Journal of cell science, 113(Pt6):955-961, 2000
Journal Title
Journal of cell science
ISSN
0021-95331477-9137
Abstract
The role of the N-terminal cleavage product of poly(ADP-ribose) polymerase (PARP) on UV mediated apoptosis was investigated in cultured HeLa cells. Ultrastructural analysis of cells expressing caspase-resistant PARP (PARP(D214A)) revealed the typical features of necrosis following UV treatment. However, cells co-expressing PARP(D214A) with the N-terminal fragment of PARP containing the DNA-binding domain underwent apoptosis instead of necrosis. In this study, we have demonstrated that the DNA-binding activity of the N-terminal fragment of PARP is important for the execution of apoptosis. Point mutations were introduced in the DNA-binding sites of the N-terminal fragment. Cells co-expressing PARP(D214A) with the mutated N-terminal fragments neither stimulated apoptosis nor prevented necrosis in response to UV irradiation. The present study proposes that the DNA-binding activity of the N-terminal fragment of PARP in UV treated cells prevents cellular ATP depletion, a mechanism by which necrotic cell death is triggered.
MeSH terms
*Apoptosis/radiation effectsBinding Sites/geneticsDNA/*genetics/metabolismGene Expression RegulationHela CellsHumansPoint MutationPoly Adenosine Diphosphate Ribose/*genetics/metabolismProtein BindingUltraviolet Rays
PMID
10683144
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Microbiology
AJOU Authors
손, 성향
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