Biochemical characterization of the RECQ4 protein, mutated in
Rothmund-Thomson syndrome.

J 2006

Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome.

MACRIS, MA, Lumír KREJČÍ, W. BUSSEN, A. SHIMAMOTO, Patrick SUNG et. al.

Základní údaje

Originální název

Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome.

Autoři

MACRIS, MA (840 Spojené státy), Lumír KREJČÍ (203 Česká republika, garant), W. BUSSEN (840 Spojené státy), A. SHIMAMOTO (392 Japonsko) a Patrick SUNG (840 Spojené státy)

Vydání

DNA Repair, 2006, 1568-7864

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 5.868

Kód RIV

RIV/00216224:14310/06:00044776

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000235089900004

Klíčová slova anglicky

recombination; DNA repair; rearrangements; genome

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 16. 9. 2010 12:26, doc. Mgr. Lumír Krejčí, Ph.D.

Anotace

V originále

Rothmund-Thomson syndrome (RTS) is an autosomal recessive disorder characterized by growth deficiency, skin and skeletal abnormalities, and a predisposition to cancer. Mutations in the RECQ4 gene, one of five human homologs of the E. coli recQ gene, have been identified in a subset of RTS patients. Cells derived from RTS patients show high levels of chromosomal instability, implicating this protein in the maintenance of genomic integrity. However, RECQ4 is the least characterized of the RecQ helicase family with regard to its molecular and catalytic properties. We have expressed the human RECQ4 protein in E. coli and purified it to near homogeneity. We show that RECQ4 has an ATPase function that is activated by DNA, with ssDNA being much more effective than dsDNA in this regard. We have determined that a DNA length of 60 nucleotides is required to maximally activate ATP hydrolysis by RECQ4, while the minimal site size for ssDNA binding by RECQ4 is between 20 and 40 nucleotides. Interestingly, RECQ4 possesses a single-strand DNA annealing activity that is inhibited by the single-strand DNA binding protein RPA. Unlike the previously characterized members of the RecQ family, RECQ4 lacks a detectable DNA helicase activity.

Návaznosti

LC06030, projekt VaV

Název: Biomolekulární centrum

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

Citovat

MACRIS, MA, Lumír KREJČÍ, W. BUSSEN, A. SHIMAMOTO a Patrick SUNG. Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome. DNA Repair. 2006, roč. 5, č. 2, 8 s. ISSN 1568-7864.

@article{898056,
   author = {Macris, MA and Krejčí, Lumír and Bussen, W. and Shimamoto, A. and Sung, Patrick},
   article_number = {2},
   keywords = {recombination; DNA repair; rearrangements; genome},
   language = {eng},
   issn = {1568-7864},
   journal = {DNA Repair},
   title = {Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome.},
   volume = {5},
   year = {2006}
}

TY  - JOUR
ID  - 898056
AU  - Macris, MA - Krejčí, Lumír - Bussen, W. - Shimamoto, A. - Sung, Patrick
PY  - 2006
TI  - Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome.
JF  - DNA Repair
VL  - 5
IS  - 2
SN  - 15687864
KW  - recombination
KW  - DNA repair
KW  - rearrangements
KW  - genome
N2  - Rothmund-Thomson syndrome (RTS) is an autosomal recessive disorder characterized by growth deficiency, skin and skeletal abnormalities, and a predisposition to cancer. Mutations in the RECQ4 gene, one of five human homologs of the E. coli recQ gene, have been identified in a subset of RTS patients. Cells derived from RTS patients show high levels of chromosomal instability, implicating this protein in the maintenance of genomic integrity. However, RECQ4 is the least characterized of the RecQ helicase family with regard to its molecular and catalytic properties. We have expressed the human RECQ4 protein in E. coli and purified it to near homogeneity. We show that RECQ4 has an ATPase function that is activated by DNA, with ssDNA being much more effective than dsDNA in this regard. We have determined that a DNA length of 60 nucleotides is required to maximally activate ATP hydrolysis by RECQ4, while the minimal site size for ssDNA binding by RECQ4 is between 20 and 40 nucleotides. Interestingly, RECQ4 possesses a single-strand DNA annealing activity that is inhibited by the single-strand DNA binding protein RPA. Unlike the previously characterized members of the RecQ family, RECQ4 lacks a detectable DNA helicase activity.
ER  -

MACRIS, MA, Lumír KREJČÍ, W. BUSSEN, A. SHIMAMOTO a Patrick SUNG. Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome. \textit{DNA Repair}. 2006, roč.~5, č.~2, 8 s. ISSN~1568-7864.

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