Hsp70 translocates to the nuclei and nucleoli, binds to XRCC1 and PARP-1, and protects HeLa cells from single-strand DNA breaks.

作者: Polychronis Kotoglou , Alexandros Kalaitzakis , Patra Vezyraki , Theodore Tzavaras , Lampros K. Michalis

DOI: 10.1007/S12192-008-0093-6

关键词:

摘要: For many years, there has been uncertainty concerning the reason for Hsp70 translocation to nucleus and nucleolus. Herein, we propose that translocates nucleoli in order participate pathways related protection of nucleoplasmic DNA or ribosomal from single-strand breaks. The absence HeLa cells, via gene silencing (knockdown), indicated essential role integrity. Therefore, depleted cells were very sensitive heat treatment their breaks multiple compared control cells. molecular mechanism with which performs its at level nucleolus during stress was examined. co-localizes PARP1 nucleus/nucleoli as observed confocal studies binds BCRT domain revealed protein–protein interaction assays. It also found simultaneously XRCC1 PARP-1, indicating function takes place repair possibly base excision system. Making a hypothetical model, have suggested is molecule interrelates creating proteins simultaneously, such XRCC1, Our data partially clarify previously unrecognized cellular response stress. Finally, can speculate plays quality integrity DNA.

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