Regulation of the human apoptotic DNase/RNase Endonuclease G: Involvement of Hsp70 and ATP

M. Kalinowska, W. Garncarz, M. Pietrowska, W. T. Garrard, P. Widlak

Research output: Contribution to journalArticlepeer-review

57 Scopus citations

Abstract

Endonuclease G (EndoG) is a mitochondrial enzyme that becomes an apoptotic nuclease when released from the mitochondrial intermembrane space. EndoG will digest either DNA or RNA, but at physiological ionic strength, RNA is a much more favorable substrate as compared to chromatin. This indicates that EndoG's major in vivo function(s) may be: (i) an apoptotic RNase, and/or (ii) an apoptotic DNase in the presence of additional co-activators. In the present study we have searched for factors that modulate the activity of human EndoG on DNA substrates. We demonstrate that EndoG forms complexes with AIF and FEN-1 but not with PCNA. Interestingly, heat shock proteins 70 interact with EndoG and are involved in the regulation of its activity. Purified Hsp70 prevented stimulation of EndoG DNase activity by other nuclear factors in the ATP-dependent manner.

Original languageEnglish (US)
Pages (from-to)821-830
Number of pages10
JournalApoptosis
Volume10
Issue number4
DOIs
StatePublished - Aug 1 2005

Keywords

  • AIF
  • Endonuclease G
  • FEN-1
  • Hsp70
  • Nuclease

ASJC Scopus subject areas

  • Pharmacology
  • Pharmaceutical Science
  • Clinical Biochemistry
  • Cell Biology
  • Biochemistry, medical
  • Cancer Research

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