Interaction of PARP2 with DNA structures mimicking DNA repair intermediates

Authors

  • M. M. Kutuzov Novosibirsk Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences 8, Akademika Lavrentieva Ave., Novosibirsk, Russian Federation, 630090 Author
  • J.-C. Ame University of Strasbourg, CNRS, ESBS Cedex Illkirch Cedex, France Author
  • S. N. Khodyreva Novosibirsk Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences 8, Akademika Lavrentieva Ave., Novosibirsk, Russian Federation, 630090 Author
  • V. Schreiber University of Strasbourg, CNRS, ESBS Cedex Illkirch Cedex, France Author
  • O. I. Lavrik Novosibirsk Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences 8, Akademika Lavrentieva Ave., Novosibirsk, Russian Federation, 630090 Author

DOI:

https://doi.org/10.7124/bc.000129

Keywords:

PARP1, PARP2, poly(ADP-ribosyl)ation, DNA binding

Abstract

Poly(ADP-ribosyl)ation is a posttranslational protein modification significant for the genomic stability and cell survival in response to DNA damage. Poly(ADP-ribosyl)ation is catalyzed by poly(ADP-ribose)polymerases (PARPs). Whereas the role of PARP1 in response to DNA damage has been widely illustrated, the contribution of another DNA-dependent PARP, PARP2, has not been studied so far. Aim. To find out specific DNA targets of PARP2. Methods. The EMSA and the PARP activity tests were used. Results. We evaluated Kd values of PARP2-DNA complexes for several DNA structures mimicking intermediates of different DNA metabolizing processes and tested these DNA as «activators» of PARP1 and PARP2 in poly(ADP-ribose) synthesis. Conclusions. Like PARP1, PARP2 does not show correlation between the activation efficiency and Kd values for DNA. PARP2 was activated most effectively in the presence of over5DNA.

References

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Published

2011-09-20

Issue

Vol. 27 No. 5 (2011)

Section

Biopolymers and Cell