There has been an internal error while processing your request. The problem has been logged and will be investigated. You may also send us an email describing how you encountered this error.
The problem may be temporary in which case you might wish to go back and try your request again or you might want to go to the home page.
First Author | Temme Claudia | Year | 2009 |
Journal | J Biol Chem | Volume | 284 |
Pages | 8337-48 | PubMed ID | 19129189 |
Abstract Text | Endonuclease G (EndoG) is a mitochondrial enzyme believed to be released during apoptosis to participate in the degradation of nuclear DNA. This paper describes a Drosophila protein, EndoGI, which inhibits EndoG specifically. EndoG and EndoGI associate with subpicomolar affinity, forming a 2:1 complex in which dimeric EndoG is bound by two tandemly repeated homologous domains of monomeric EndoGI. Binding appears to involve the active site of EndoG. EndoGI is present in the cell nucleus at micromolar concentrations. Upon induction of apoptosis, levels of the inhibitor appear to be reduced, and it is relocalized to the cytoplasm. EndoGI, encoded by the predicted open reading frame cg4930, is expressed throughout Drosophila development. Flies homozygous for a hypomorphic EndoGI mutation have a strongly reduced viability, which is modulated by genetic background and diet. We propose that EndoGI protects the cell against low levels of EndoG outside mitochondria. | Doi | 10.1074/jbc.M808319200 |
Issue | 13 | Month | Mar |