A DNA helicase from Xenopus laevis ovaries - PubMed (original) (raw)
. 1988 Nov 29;27(24):8701-6.
doi: 10.1021/bi00424a002.
Affiliations
- PMID: 2853968
- DOI: 10.1021/bi00424a002
A DNA helicase from Xenopus laevis ovaries
E H Poll et al. Biochemistry. 1988.
Erratum in
- Biochemistry 1989 Feb 21;28(4):1930
Abstract
A DNA helicase was extensively purified from Xenopus laevis ovaries. The most purified fraction was free of DNA topoisomerase, DNA polymerase, and nuclease activities. The enzyme had a Stokes radius of 54 A and a sedimentation coefficient of 6-7.3 S, from which a native molecular weight of 140,000-170,000 was calculated. DNA helicase activity required Mg2+ or Mn2+ and was dependent on hydrolysis of ATP or dATP. Monovalent cations, K+ and Na+, stimulated DNA unwinding with an optimum at 130 mM. DNA-dependent ATPase activity copurified with the X. laevis DNA helicase. Double-stranded and single-stranded DNA were both cofactors for the ATPase activity, but single-stranded DNA was more efficient. The molecular weight, monovalent cation dependence, cofactor requirements, and elution from single-stranded DNA-cellulose suggest that the X. laevis DNA helicase is different from previously described eukaryotic DNA helicases.
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