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  Crystal structure of the EndoG/EndoGI complex: mechanism of EndoG inhibition

Loll, B., Gebhardt, M., Wahle, E., & Meinhart, A. (2009). Crystal structure of the EndoG/EndoGI complex: mechanism of EndoG inhibition. Nucleic Acids Research (London), 37(21), 7312-7320. doi:10.1093/nar/gkp770.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-11A1-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-11A2-F
Genre: Journal Article
Alternative Title : Crystal structure of the EndoG/EndoGI complex: mechanism of EndoG inhibition

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 Creators:
Loll, Bernhard1, Author              
Gebhardt, Maike1, Author              
Wahle, Elmar, Author
Meinhart, Anton1, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: EndoG is a ubiquitous nuclease that is translocated into the nucleus during apoptosis to participate in DNA degradation. The enzyme cleaves double- and single-stranded DNA and RNA. Related nucleases are found in eukaryotes and prokaryotes, which have evolved sophisticated mechanisms for genome protection against self-antagonizing nuclease activity. Common mechanisms of inhibition are secretion, sequestration into a separate cellular compartment or by binding to protein inhibitors. Although EndoG is silenced by compartmentalization into the mitochondrial intermembrane space, a nucleus-localized protein inhibitor protects cellular polynucleotides from degradation by stray EndoG under non-apoptotic conditions in Drosophila. Here, we report the first three-dimensional structure of EndoG in complex with its inhibitor EndoGI. Although the mechanism of inhibition is reminiscent of bacterial protein inhibitors, EndoGI has evolved independently from a generic protein-protein interaction module. EndoGI is a two-domain protein that binds the active sites of two monomers of EndoG, with EndoG being sandwiched between EndoGI. Since the amino acid sequences of eukaryotic EndoG homologues are highly conserved, this model is valid for eukaryotic dimeric EndoG in general. The structure indicates that the two active sites of EndoG occupy the most remote spatial position possible at the molecular surface and a concerted substrate processing is unlikely.

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Language(s): eng - English
 Dates: 2009-08-302009-08-072009-09-012009-09-252009-11-01
 Publication Status: Published in print
 Pages: 9
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 Table of Contents: -
 Rev. Type: Peer
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Title: Nucleic Acids Research (London)
  Other : Nucleic Acids Res
Source Genre: Journal
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Publ. Info: Oxford : Oxford University Press
Pages: - Volume / Issue: 37 (21) Sequence Number: - Start / End Page: 7312 - 7320 Identifier: ISSN: 0305-1048
CoNE: https://pure.mpg.de/cone/journals/resource/110992357379342