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, Margaret, Lumír KREJČÍ, Wendy BUSSEN, Akira SHIMAMOTO, Patrick SUNG et. al.

Basic information

Original name

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

Name in Czech

Biochemická charakterizace proteinu RECQ4, mutovaného u Rothmund-Thpomson syndromu

Authors

MACRIS, Margaret, Lumír KREJČÍ, Wendy BUSSEN, Akira SHIMAMOTO and Patrick SUNG

Edition

DNA Repair, ELSEVIER, 2006, 1568-7864

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 5.868

Organization unit

Faculty of Science

UT WoS

000235089900004

Keywords in English

RTS; RECQ4; ATPase; Helicase; ssDNA annealing; DNA repair

Abstract

ORIG CZ

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.

In Czech

Článek popisuje základní biochemickou charakterizaci proteinu RECQ4

Links

LC06030, research and development project

Name: Biomolekulární centrum

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre

ME 888, research and development project

Name: Srs2 protein a jeho multifunkční úloha při rekombinančních /opravných procesech

Investor: Ministry of Education, Youth and Sports of the CR, Srs2 protein and its multi-functional role in rekombination/repair processes

MSM0021622413, plan (intention)

Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment

Citovat

MACRIS, Margaret, Lumír KREJČÍ, Wendy BUSSEN, Akira SHIMAMOTO and Patrick SUNG. Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome. DNA Repair. ELSEVIER, 2006, vol. 2, No 5, p. 172-180, 8 pp. ISSN 1568-7864.

@article{699834,
   author = {Macris, Margaret and Krejčí, Lumír and Bussen, Wendy and Shimamoto, Akira and Sung, Patrick},
   article_number = {5},
   keywords = {RTS; RECQ4; ATPase; Helicase; ssDNA annealing; DNA repair},
   language = {eng},
   issn = {1568-7864},
   journal = {DNA Repair},
   title = {Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome},
   url = {http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6X17-4H8MP0Y-3&_coverDate=02%2F03%2F2006&_alid=478345836&_rdoc=1&_fmt=&_orig=search&_qd=1&_cdi=7235&_sort=d&view=c&_acct=C000045159&_version=1&_urlVersion=0&_userid=835458&md5=ba3169debebeffbec2b5},
   volume = {2},
   year = {2006}
}

TY  - JOUR
ID  - 699834
AU  - Macris, Margaret - Krejčí, Lumír - Bussen, Wendy - Shimamoto, Akira - Sung, Patrick
PY  - 2006
TI  - Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome
JF  - DNA Repair
VL  - 2
IS  - 5
SP  - 172-180
EP  - 172-180
PB  - ELSEVIER
SN  - 15687864
KW  - RTS
KW  - RECQ4
KW  - ATPase
KW  - Helicase
KW  - ssDNA annealing
KW  - DNA repair
UR  - http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6X17-4H8MP0Y-3&_coverDate=02%2F03%2F2006&_alid=478345836&_rdoc=1&_fmt=&_orig=search&_qd=1&_cdi=7235&_sort=d&view=c&_acct=C000045159&_version=1&_urlVersion=0&_userid=835458&md5=ba3169debebeffbec2b5
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, Margaret, Lumír KREJČÍ, Wendy BUSSEN, Akira SHIMAMOTO and Patrick SUNG. Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome. \textit{DNA Repair}. ELSEVIER, 2006, vol.~2, No~5, p.~172-180, 8 pp. ISSN~1568-7864.

Detailed Information on Publication Record