The DNA topoisomerase IIbeta binding protein 1 (TopBP1) interacts with poly (ADP-ribose) polymerase (PARP-1)
| Autor: | Yvonne Wollmann, Peter F. Zipfel, Hanspeter Saluz, Frank Hänel, Uta Schmidt, Gerhard D. Wieland |
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| Rok vydání: | 2007 |
| Předmět: |
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DNA polymerase II Poly ADP ribose polymerase Kruppel-Like Transcription Factors Poly (ADP-Ribose) Polymerase-1 Biology Biochemistry DNA polymerase delta Humans Immunoprecipitation Molecular Biology Replication protein A Cell Nucleus Adenosine Diphosphate Ribose DNA clamp Binding Sites DNA replication Nuclear Proteins Cell Biology Molecular biology Proliferating cell nuclear antigen Protein Structure Tertiary DNA-Binding Proteins biology.protein Poly(ADP-ribose) Polymerases Carrier Proteins HeLa Cells |
| Zdroj: | Journal of cellular biochemistry. 102(1) |
| ISSN: | 0730-2312 |
| Popis: | We investigated the physical association of the DNA topoisomerase IIβ binding protein 1 (TopBP1), involved in DNA replication and repair but also in regulation of apoptosis, with poly(ADP-ribose) polymerase-1 (PARP-1). This enzyme plays a crucial role in DNA repair and interacts with many DNA replication/repair factors. It was shown that the sixth BRCA1 C-terminal (BRCT) domain of TopBP1 interacts with a protein fragment of PARP-1 in vitro containing the DNA-binding and the automodification domains. More significantly, the in vivo interaction of endogenous TopBP1 and PARP-1 proteins could be shown in HeLa-S3 cells by co-immunoprecipitation. TopBP1 and PARP-1 are localized within overlapping regions in the nucleus of HeLa-S3 cells as shown by immunofluorescence. Exposure to UVB light slightly enhanced the interaction between both proteins. Furthermore, TopBP1 was detected in nuclear regions where poly(ADP-ribose) (PAR) synthesis takes place and is ADP-ribosylated by PARP-1. Finally, cellular (ADP-ribosyl)ating activity impairs binding of TopBP1 to Myc-interacting zinc finger protein-1 (Miz-1). The results indicate an influence of post-translational modifications of TopBP1 on its function during DNA repair. J. Cell. Biochem. 102: 171–182, 2007. © 2007 Wiley-Liss, Inc. |
| Databáze: | OpenAIRE |
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