RECQ4 selectively recognizes Holliday junctions |
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| Affiliation: | 1. Department of Biology, Masaryk University, Brno, Czech Republic;2. National Centre for Biomolecular Research, Masaryk University, Brno, Czech Republic;3. International Clinical Research Center, Center for Biomolecular and Cellular Engineering, St. Anne''s University Hospital Brno, Brno, Czech Republic;1. Drug Safety Research Laboratories, Astellas Pharma Inc., 2-1-6 Kashima Yodogawa-ku, Osaka 532-8514, Japan;2. Present address: Laboratory of Laboratory Animal Science and Medicine, Graduate School of Veterinary Medicine, Hokkaido University, Kita 18, Nishi 9, Kita-ku, Sapporo 060-0818, Japan;3. Present address: Research Administration Office, Kyoto University, Yoshida-honmachi, Sakyo-ku, Kyoto 606-8501, Japan;4. Present address: Drug Safety Research Laboratories, Shin Nippon Biomedical Laboratories, Ltd., 2-1-1 Fushimi-machi, Chuo-ku, Osaka 541-0044, Japan;1. Laboratory of DNA Damage Signaling, Department of Late Effects Studies, Radiation Biology Center, Kyoto University, Kyoto, Japan;;2. Department of Cell Transplantation and Regenerative Medicine, Tokai University School of Medicine, Isehara, Japan;;3. Cancer Genomics Project, Graduate School of Medicine;4. Laboratory of DNA Information Analysis, The University of Tokyo, Tokyo, Japan;5. Laboratory of Sequence Analysis, Human Genome Center, Institute of Medical Science, The University of Tokyo, Tokyo, Japan;;6. Department of Environmental Sciences and Engineering, University of North Carolina at Chapel Hill, Chapel Hill, NC;;7. Department of Pediatrics, Nagoya University Graduate School of Medicine, Nagoya, Japan;;8. Department of Pathology and Tumor Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan;9. Department of Preventive Medicine, Kyushu University Faculty of Medical Sciences, Fukuoka, Japan;3. Feinberg School of Medicine and;5. Robert H. Lurie Comprehensive Cancer Center, Northwestern University, Chicago, Illinois 60611 and;4. Jesse Brown Veterans Affairs Medical Center, Chicago, Illinois 60612;3. Department of Environment and Primary Prevention, Istituto Superiore di Sanità, 00161 Roma, Italy;4. Department of Science, University Roma Tre, 00154 Roma, Italy;1. Department of Biology, Masaryk University, Brno, Czech Republic;2. International Clinical Research Center, Center for Biomolecular and Cellular Engineering, St. Anne''s University Hospital Brno, Brno, Czech Republic;3. National Centre for Biomolecular Research, Masaryk University, Brno, Czech Republic |
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| Abstract: | 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 322–400 aa 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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| Keywords: | Genomic stability Homologous recombination RECQ4 DNA binding Holliday junction |
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