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The role of DFF40-CAD endonuclease during terminal stages of apoptosis

100%

Widlak P.

Cellular and Molecular Biology Letters

2000

tom 05

nr 2

Bim: guardian of tissue homeostasis and critical regulator of the immune system, tumorigenesis and bone biology

84%

Akiyama T. , Tanaka S.

Archivum Immunologiae et Therapiae Experimentalis

2011

tom 59

nr 4

Expression of connexins 26, 32 and 43 in the human colon - an immunohistochemical study

84%

Kanczuga-Koda L. , Sulkowski S. , Koda M. , Sobaniec-Lotowska M. , Sulkowska M.

Folia Histochemica et Cytobiologica

2004

tom 42

nr 4

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

84%

Kalinowska-Herok M. , Widlak P.

Acta Biochimica Polonica

2008

tom 55

nr 1

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.