Characterization of the Properties of a Human Homologue of Escherichia coli RecQ from Xeroderma Pigmentosum Group C and from HeLa Cells

Cell Structure and Function

Michio Ui¹  Takemi Enomoto¹  Atsuko Miyajima¹  Shusuke Tada¹  Masayuki Seki¹  Tadao Sonoyama¹  Jim Yanagisawa¹ 

[1] Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, University of Tokyo

关键词: DNA helicase Q1;    human homologue;    RecQ;    xeroderma pigmentosum;    complementation group C cells;    HeLa cells;   

DOI  :  10.1247/csf.21.123

学科分类：分子生物学，细胞生物学和基因

来源: Japan Society for Cell Biology

【 摘 要 】

References(35)Cited-By(6)We showed that DNA-dependent ATPase Ql (DNA helicase Ql) from xeroderma pignientosiim complementation group C (XP-C) cells elutes from FPLC Mono Q column at higher concentrations of KC1 than that from other human cells (35). We purified DNA helicase Ql from XP-C and HeLa cells. The purified fractions of both cells contained a major polypeptide with a molecular mass of 73 kDa and had the same enzymatic properties, including salt- and temperature-sensitivity. Characterization using an anti-DNA helicase Ql antibody indicated that this enzyme localized in the nuclei and was not modified by incorporating phosphate groups through phosphorylation and ADP-ribosylation. No interactions of DNA helicase Ql with other proteins were indicated by immunoprecipitation of the helicase from crude extracts. No difference was observed in XP-C cells in intracellular localization of DNA helicase Ql, phosphorylation, and the interaction with other proteins as compared to HeLa cells.

【 授权许可】

Unknown