Other formats:
BibTeX
LaTeX
RIS
@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.
|
