SEDLÁČKOVÁ, Hana, Barbora CECHOVA, Jarmila MLČOUŠKOVÁ and Lumír KREJČÍ. RECQ4 selectively recognizes Holliday junctions. DNA Repair. Amsterdam: ELSEVIER SCIENCE BV, 2015, vol. 30, "neuvedeno", p. 80-89. ISSN 1568-7864. Available from: https://dx.doi.org/10.1016/j.dnarep.2015.02.020.
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Basic information
Original name RECQ4 selectively recognizes Holliday junctions
Authors SEDLÁČKOVÁ, Hana (203 Czech Republic, belonging to the institution), Barbora CECHOVA (203 Czech Republic), Jarmila MLČOUŠKOVÁ (203 Czech Republic, belonging to the institution) and Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution).
Edition DNA Repair, Amsterdam, ELSEVIER SCIENCE BV, 2015, 1568-7864.
Other information
Original language English
Type of outcome Article in a journal
Field of Study Genetics and molecular biology
Country of publisher Netherlands
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 3.929
RIV identification code RIV/00216224:14110/15:00080936
Organization unit Faculty of Medicine
Doi http://dx.doi.org/10.1016/j.dnarep.2015.02.020
UT WoS 000355050800009
Keywords in English Genomic stability; Homologous recombination; RECQ4; DNA binding; Holliday junction
Tags EL OK, podil
Tags International impact, Reviewed
Changed by Changed by: Ing. Mgr. Věra Pospíšilíková, učo 9005. Changed: 29/7/2015 13:11.
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. (C) 2015 Elsevier B.V. All rights reserved.
Links
EE2.3.30.0037, research and development projectName: Zaměstnáním nejlepších mladých vědců k rozvoji mezinárodní spolupráce
GAP207/12/2323, research and development projectName: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I
Investor: Czech Science Foundation
GA13-26629S, research and development projectName: SUMO a stability genomu
Investor: Czech Science Foundation
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