We showed that DNA-dependent ATPase Q1 (DNA helicase Q1) from xeroderma pigmentosum complementation group C (XP-C) cells elutes from FPLC Mono Q column at higher concentrations of KCl than that from other human cells (35). We purified DNA helicase Q1 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 Q1 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 Q1 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 Q1, phosphorylation, and the interaction with other proteins as compared to HeLa cells.
No takes yet. Share an insight, caveat, or question.
Tada et al. (1996) studied this question.
Synapse has enriched 3 closely related papers on similar clinical questions. Consider them for comparative context: