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Endonuclease G: a mitochondrial protein released in apoptosis and involved in caspase-independent DNA degradation.
- Source :
-
Cell Death & Differentiation . Dec2001, Vol. 8 Issue 12, p1136. 7p. - Publication Year :
- 2001
-
Abstract
- A hallmark of apoptosis is the fragmentation of nuclear DNA. Although this activity involves the caspase-3-dependent DNAse CAD (caspase-activated DNAse), evidence exists that DNA fragmentation can occur independently of caspase activity. Here we report on the ability of truncated Bid (tBid) to induce the release of a DNAse activity from mitochondria. This DNAse activity was identified by mass spectrometry as endonuclease G, an abundant 30 kDa protein released from mitochondria under apoptotic conditions. No tBid-induced endonuclease G release could be observed in mitochondria from Bcl-2-transgenic mice. The in vivo occurrence of endonuclease G release from mitochondria during apoptosis was confirmed in the liver from mice injected with agonistic anti-Fas antibody and is completely prevented in Bcl-2 transgenic mice. These data indicate that endonuclease G may be involved in CAD-independent DNA fragmentation during cell death pathways in which truncated Bid is generated. [ABSTRACT FROM AUTHOR]
- Subjects :
- *ENDONUCLEASES
*MITOCHONDRIA
*APOPTOSIS
Subjects
Details
- Language :
- English
- ISSN :
- 13509047
- Volume :
- 8
- Issue :
- 12
- Database :
- Academic Search Index
- Journal :
- Cell Death & Differentiation
- Publication Type :
- Academic Journal
- Accession number :
- 8851246
- Full Text :
- https://doi.org/10.1038/sj.cdd.4400944