RECQ4 selectively recognizes Holliday junctions

J 2015

RECQ4 selectively recognizes Holliday junctions

SEDLÁČKOVÁ, Hana, Barbora CECHOVA, Jarmila MLČOUŠKOVÁ a Lumír KREJČÍ

Základní údaje

Originální název

RECQ4 selectively recognizes Holliday junctions

Autoři

SEDLÁČKOVÁ, Hana (203 Česká republika, domácí), Barbora CECHOVA (203 Česká republika), Jarmila MLČOUŠKOVÁ (203 Česká republika, domácí) a Lumír KREJČÍ (203 Česká republika, garant, domácí)

Vydání

DNA Repair, Amsterdam, ELSEVIER SCIENCE BV, 2015, 1568-7864

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

Genetika a molekulární biologie

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 3.929

Kód RIV

RIV/00216224:14110/15:00080936

Organizační jednotka

Lékařská fakulta

DOI

http://dx.doi.org/10.1016/j.dnarep.2015.02.020

UT WoS

000355050800009

Klíčová slova anglicky

Genomic stability; Homologous recombination; RECQ4; DNA binding; Holliday junction

Štítky

EL OK, podil

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 29. 7. 2015 13:11, Ing. Mgr. Věra Pospíšilíková

Anotace

V originále

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.

Návaznosti

EE2.3.30.0037, projekt VaV

Název: Zaměstnáním nejlepších mladých vědců k rozvoji mezinárodní spolupráce

GAP207/12/2323, projekt VaV

Název: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I

Investor: Grantová agentura ČR, Endonuleázová a translokázová aktivita v restrikčních-modifikačních komplexech typu I

GA13-26629S, projekt VaV

Název: SUMO a stability genomu

Investor: Grantová agentura ČR, SUMO a stability genomu

Citovat

SEDLÁČKOVÁ, Hana, Barbora CECHOVA, Jarmila MLČOUŠKOVÁ a Lumír KREJČÍ. RECQ4 selectively recognizes Holliday junctions. DNA Repair. Amsterdam: ELSEVIER SCIENCE BV, 2015, roč. 30, "neuvedeno", s. 80-89. ISSN 1568-7864. Dostupné z: https://dx.doi.org/10.1016/j.dnarep.2015.02.020.

@article{1306996,
   author = {Sedláčková, Hana and Cechova, Barbora and Mlčoušková, Jarmila and Krejčí, Lumír},
   article_location = {Amsterdam},
   article_number = {"neuvedeno"},
   doi = {http://dx.doi.org/10.1016/j.dnarep.2015.02.020},
   keywords = {Genomic stability; Homologous recombination; RECQ4; DNA binding; Holliday junction},
   language = {eng},
   issn = {1568-7864},
   journal = {DNA Repair},
   title = {RECQ4 selectively recognizes Holliday junctions},
   volume = {30},
   year = {2015}
}

TY  - JOUR
ID  - 1306996
AU  - Sedláčková, Hana - Cechova, Barbora - Mlčoušková, Jarmila - Krejčí, Lumír
PY  - 2015
TI  - RECQ4 selectively recognizes Holliday junctions
JF  - DNA Repair
VL  - 30
IS  - "neuvedeno"
SP  - 80-89
EP  - 80-89
PB  - ELSEVIER SCIENCE BV
SN  - 15687864
KW  - Genomic stability
KW  - Homologous recombination
KW  - RECQ4
KW  - DNA binding
KW  - Holliday junction
N2  - 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.
ER  -

SEDLÁČKOVÁ, Hana, Barbora CECHOVA, Jarmila MLČOUŠKOVÁ a Lumír KREJČÍ. RECQ4 selectively recognizes Holliday junctions. \textit{DNA Repair}. Amsterdam: ELSEVIER SCIENCE BV, 2015, roč.~30, ''neuvedeno'', s.~80-89. ISSN~1568-7864. Dostupné z: https://dx.doi.org/10.1016/j.dnarep.2015.02.020.

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