Abstract |
The RecQ family of DNA helicases including WRN ( Werner syndrome protein) and BLM ( Bloom syndrome protein) protects the genome against deleterious changes. Here we report the cocrystal structure of the RecQ C-terminal (RQC) domain of human WRN bound to a DNA duplex. In the complex, the RQC domain specifically interacted with a blunt end of the duplex and, surprisingly, unpaired a Watson-Crick base pair in the absence of an ATPase domain. The beta wing, an extended hairpin motif that is characteristic of winged-helix motifs, was used as a "separating knife" to wedge between the first and second base pairs, whereas the recognition helix, a principal component of helix-turn-helix motifs that are usually embedded within DNA grooves, was unprecedentedly excluded from the interaction. Our results demonstrate a function of the winged-helix motif central to the helicase reaction, establishing the first structural paradigm concerning the DNA structure-specific activities of the RecQ helicases.
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Authors | Ken Kitano, Sun-Yong Kim, Toshio Hakoshima |
Journal | Structure (London, England : 1993)
(Structure)
Vol. 18
Issue 2
Pg. 177-87
(Feb 10 2010)
ISSN: 1878-4186 [Electronic] United States |
PMID | 20159463
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | Copyright 2010 Elsevier Ltd. All rights reserved. |
Chemical References |
- DNA
- Exodeoxyribonucleases
- RecQ Helicases
- WRN protein, human
- Werner Syndrome Helicase
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Topics |
- Amino Acid Sequence
- Animals
- Base Sequence
- Crystallography, X-Ray
- DNA
(chemistry, metabolism)
- Exodeoxyribonucleases
(chemistry, genetics, metabolism)
- Humans
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis
- Nucleic Acid Conformation
- Protein Structure, Secondary
- Protein Structure, Tertiary
- RecQ Helicases
(chemistry, genetics, metabolism)
- Sequence Alignment
- Werner Syndrome
(genetics, metabolism)
- Werner Syndrome Helicase
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