RECQ4 selectively recognizes Holliday junctions

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14110%2F15%3A00080936" target="_blank" >RIV/00216224:14110/15:00080936 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00159816:_____/15:00062876

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.dnarep.2015.02.020" target="_blank" >http://dx.doi.org/10.1016/j.dnarep.2015.02.020</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.dnarep.2015.02.020" target="_blank" >10.1016/j.dnarep.2015.02.020</a>

Jazyk výsledku

angličtina

Název v původním jazyce

RECQ4 selectively recognizes Holliday junctions

Popis výsledku v původním jazyce

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. Thesesyndromes 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.

Název v anglickém jazyce

RECQ4 selectively recognizes Holliday junctions

Popis výsledku anglicky

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. Thesesyndromes 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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

—

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

DNA Repair

ISSN

1568-7864

e-ISSN

—

Svazek periodika

30

Číslo periodika v rámci svazku

"neuvedeno"

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

10

Strana od-do

80-89

Kód UT WoS článku

000355050800009

EID výsledku v databázi Scopus

—