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Human Molecular Genetics, 2002, Vol. 11, No. 19 2319-2329
© 2002 Oxford University Press

Poly(ADP-ribose) polymerase 2 localizes to mammalian active centromeres and interacts with PARP-1, Cenpa, Cenpb and Bub3, but not Cenpc

Alka Saxena1, Lee H. Wong1, Paul Kalitsis1, Elizabeth Earle1, Lisa G. Shaffer2 and K.H. Andy Choo1,*

1The Murdoch Childrens Research Institute, Royal Children's Hospital, Flemington Road, Parkville 3052, Australia and 2Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA

Received May 21, 2002; Accepted July 17, 2002

Poly(ADP-ribose) polymerase 2 (PARP-2) is a newly discovered member of the PARP family. We report the association of PARP-2 with mammalian centromeres in a cell-cycle-dependent manner, accumulating at centromeres during prometaphase and metaphase, disassociating during anaphase, and disappearing from the centromeres by telophase. Analysis of a pseudodicentric chromosome and a human neocentromere indicates that PARP-2 binding occurs only at active centromeres in a sequence-independent manner. Centromere binding peaks at the outer centromere region, and is significantly enhanced upon treatment with microtubule-inhibiting drugs. Co-immunoprecipitation assay demonstrates interaction between PARP-2 and its functional homolog PARP-1, constitutive centromere proteins Cenpa and Cenpb, and spindle checkpoint protein Bub3, but not with a third constitutive centromere protein Cenpc. These results, together with our previous demonstration that PARP-1 displays an identical binding pattern with Cenpa, Cenpb and Bub3, but not Cenpc, and that all three proteins undergo significant poly(ADP-ribosyl)ation upon {gamma}-irradiation of cells, point to possible diverse roles of PARP-2 and PARP-1 in modulating the structure and checkpoint functions of the mammalian centromere, in particular during radiation-induced DNA damage.

* To whom correspondence should be addressed. Tel: +61 383416306; Fax: +61 393481391; Email: choo{at}cryptic.rch.unimelb.edu.au


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