RECQ4 selectively recognizes Holliday junctions
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
25769792
DOI
10.1016/j.dnarep.2015.02.020
PII: S1568-7864(15)00056-7
Knihovny.cz E-zdroje
- Klíčová slova
- DNA binding, Genomic stability, Holliday junction, Homologous recombination, RECQ4,
- MeSH
- helikasy RecQ chemie metabolismus MeSH
- homologní rekombinace MeSH
- křížová struktura DNA metabolismus MeSH
- lidé MeSH
- multimerizace proteinu MeSH
- replikace DNA MeSH
- sekvence nukleotidů MeSH
- terciární struktura proteinů MeSH
- vazebná místa MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- helikasy RecQ MeSH
- křížová struktura DNA MeSH
- RECQL4 protein, human MeSH Prohlížeč
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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