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  Human Holliday junction resolvase GEN1 uses a chromodomain for efficient DNA recognition and cleavage

Lee, S.-H., Princz, L. N., Klügel, M. F., Habermann, B., Pfander, B., & Biertuempfel, C. (2015). Human Holliday junction resolvase GEN1 uses a chromodomain for efficient DNA recognition and cleavage. eLife, 4: e12256. doi:10.7554/eLife.12256.

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 Creators:
Lee, Shun-Hsiao1, Author              
Princz, Lissa Nicola2, Author              
Klügel, Maren Felizitas1, Author              
Habermann, Bianca3, Author              
Pfander, Boris2, Author              
Biertuempfel, Christian1, Author              
Affiliations:
1Biertümpfel, Christian / Molecular Mechanisms of DNA Repair, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565143              
2Pfander, Boris / DNA Replication and Genome Integrity, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565165              
3Habermann, Bianca / Computational Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1832284              

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 Abstract: Holliday junctions (HJs) are key DNA intermediates in homologous recombination. They link homologous DNA strands and have to be faithfully removed for proper DNA segregation and genome integrity. Here, we present the crystal structure of human HJ resolvase GEN1 complexed with DNA at 3.0 Å resolution. The GEN1 core is similar to other Rad2/XPG nucleases. However, unlike other members of the superfamily, GEN1 contains a chromodomain as an additional DNA interaction site. Chromodomains are known for their chromatin-targeting function in chromatin remodelers and histone(de)acetylases but they have not previously been found in nucleases. The GEN1 chromodomain directly contacts DNA and its truncation severely hampers GEN1's catalytic activity. Structure-guided mutations in vitroand in vivo in yeast validated our mechanistic findings. Our study provides the missing structure in the Rad2/XPG family and insights how a well-conserved nuclease core acquires versatility in recognizing diverse substrates for DNA repair and maintenance.

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Language(s): eng - English
 Dates: 2015-12-18
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.7554/eLife.12256
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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: 4 Sequence Number: e12256 Start / End Page: - Identifier: Other: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X