High mobility group proteins stimulate DNA cleavage by apoptotic endonuclease DFF40-CAD due to HMG-box interactions with DNA

• Autorzy: Kalinowska-Herok M. , Widlak P.
• Języki publikacji: EN

Abstrakty

EN

The DFF40/CAD endonuclease is primarily responsible for internucleosomal DNA cleavage during the terminal stages of apoptosis. It has been previously demonstrated that the major HMG-box-containing chromatin proteins HMGB1 and HMGB2 stimulate naked DNA cleavage by DFF40/CAD. Here we investigate the mechanism of this stimulation and show that HMGB1 neither binds to DFF40/CAD nor enhances its ability for stable binding to DNA. Comparison of the stimulatory activities of different truncated forms of HMGB1 protein indicates that a structural array of two HMG-boxes is required for such stimulation. HMG-boxes are known to confer specific local distortions of DNA structure upon binding. Interestingly, the presence of DNA strand cross-links formed by cisplatin or transplatin, which may somehow mimic distortions induced by HMG-boxes, also affects DNA cleavage by the nuclease. The data presented suggest that changes induced in DNA conformation upon HMG-box binding makes the substrate more accessible to cleavage by DFF40/CAD nuclease and thus may contribute to preferential linker DNA cleavage during apoptosis.

Słowa kluczowe

EN

DNA fragmentation factor; nuclease; caspase-activated DNase; apoptosis; HMGB1 protein; chromatin; tissue homeostasis; cisplatin

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2008
• Tom: 55
• Numer: 1
• Opis fizyczny: p.21-26,fig.,ref.

Twórcy

autor

Kalinowska-Herok M.

• Maria Sklodowska-Curie Cancer Center and Institute of Oncology, 44-100 Gliwice, Poland

autor

Widlak P.

Bibliografia

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