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  The Mre11:Rad50 structure shows an ATP-dependent molecular clamp in DNA double-strand break repair.

Lammens, K., Bemeleit, D. J., Moeckel, C., Clausing, E., Schele, A., Hartung, S., et al. (2011). The Mre11:Rad50 structure shows an ATP-dependent molecular clamp in DNA double-strand break repair. Cell, 145(1), 54-66. doi:10.1016/j.cell.2011.02.038.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0017-8CB4-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-DB83-3
Genre: Journal Article

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 Creators:
Lammens, K.1, Author
Bemeleit, D. J.1, Author
Moeckel, C.1, Author
Clausing, E.1, Author
Schele, A.1, Author
Hartung, S.1, Author
Schiller, C. B.1, Author
Lucas, M.1, Author
Angermueller, C.1, Author
Söding, J.2, Author              
Straesser, K.1, Author
Hopfner, K. P.1, Author
Affiliations:
1external, ou_persistent22              
2Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1933286              

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 Abstract: The MR (Mre11 nuclease and Rad50 ABC ATPase) complex is an evolutionarily conserved sensor for DNA double-strand breaks, highly genotoxic lesions linked to cancer development. MR can recognize and process DNA ends even if they are blocked and misfolded. To reveal its mechanism, we determined the crystal structure of the catalytic head of Thermotoga maritima MR and analyzed ATP-dependent conformational changes. MR adopts an open form with a central Mre11 nuclease dimer and two peripheral Rad50 molecules, a form suited for sensing obstructed breaks. The Mre11 C-terminal helix-loop-helix domain binds Rad50 and attaches flexibly to the nuclease domain, enabling large conformational changes. ATP binding to the two Rad50 subunits induces a rotation of the Mre11 helix-loop-helix and Rad50 coiled-coil domains, creating a clamp conformation with increased DNA-binding activity. The results suggest that MR is an ATP-controlled transient molecular clamp at DNA double-strand breaks.

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Language(s): eng - English
 Dates: 2011
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.cell.2011.02.038
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Title: Cell
Source Genre: Journal
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Pages: - Volume / Issue: 145 (1) Sequence Number: - Start / End Page: 54 - 66 Identifier: ISSN: 0092-8674