RECQ4 selectively recognizes Holliday junctions
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
25769792
DOI
10.1016/j.dnarep.2015.02.020
PII: S1568-7864(15)00056-7
Knihovny.cz E-resources
- Keywords
- DNA binding, Genomic stability, Holliday junction, Homologous recombination, RECQ4,
- MeSH
- RecQ Helicases chemistry metabolism MeSH
- Homologous Recombination MeSH
- DNA, Cruciform metabolism MeSH
- Humans MeSH
- Protein Multimerization MeSH
- DNA Replication MeSH
- Base Sequence MeSH
- Protein Structure, Tertiary MeSH
- Binding Sites MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- RecQ Helicases MeSH
- DNA, Cruciform MeSH
- RECQL4 protein, human MeSH Browser
The RECQ4 protein belongs to the RecQ helicase family, which plays crucial roles in genome maintenance. Mutations in the RECQ4 gene are associated with three insidious hereditary disorders: Rothmund-Thomson, Baller-Gerold, and RAPADILINO syndromes. These syndromes are characterized by growth deficiency, radial ray defects, red rashes, and higher predisposition to malignancy, especially osteosarcomas. Within the RecQ family, RECQ4 is the least characterized, and its role in DNA replication and repair remains unknown. We have identified several DNA binding sites within RECQ4. Two are located at the N-terminus and one is located within the conserved helicase domain. N-terminal domains probably cooperate with one another and promote the strong annealing activity of RECQ4. Surprisingly, the region spanning 322-400aa shows a very high affinity for branched DNA substrates, especially Holliday junctions. This study demonstrates biochemical activities of RECQ4 that could be involved in genome maintenance and suggest its possible role in processing replication and recombination intermediates.
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