PMID: 7543199Jul 11, 1995Paper

Purification and properties of human DNA helicase VI

Nucleic Acids Research
Narendra TutejaA Falaschi

Abstract

A novel ATP-dependent DNA unwinding enzyme, called human DNA helicase VI (HDH VI), was purified to apparent homogeneity from HeLa cells and characterized. From 327 g of cultured cells, 0.44 mg of pure enzyme was recovered, free of DNA polymerase, ligase, topoisomerase, nicking and nuclease activities. The enzyme behaves as a monomer having an M(r) of 128 kDa, whether determined with SDS-PAGE, or in native conditions. Photoaffinity labelling with [alpha-32P]ATP labelled the 128 kDa protein. Only ATP or dATP hydrolysis supports the unwinding activity for which a divalent cation (Mg2+ > Mn2+) is required. HDH VI unwinds exclusively DNA duplexes with an annealed portion < 32 bp and prefers a replication fork-like structure of the substrate. It cannot unwind blunt-end duplexes and is inactive also on DNA-RNA or RNA-RNA hybrids. HDH VI unwinds DNA unidirectionally by moving in the 3' to 5' direction along the bound strand.

References

Jun 1, 1992·Chromosoma·P Thömmes, U Hübscher
Jul 11, 1991·Nucleic Acids Research·N TutejaA Falaschi
Dec 11, 1990·Nucleic Acids Research·N TutejaA Falaschi
Jan 1, 1990·Annual Review of Biochemistry·S W Matson, K A Kaiser-Rogers
Oct 9, 1987·Biochimica Et Biophysica Acta·H Stahl, R Knippers
Jan 1, 1981·Annual Review of Biochemistry·K Geider, H Hoffmann-Berling
Jul 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·H P Ottiger, U Hübscher
Apr 11, 1994·Nucleic Acids Research·A GeorgakiU Hübscher
May 25, 1993·Nucleic Acids Research·N TutejaA Falaschi

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Citations

May 1, 1996·Nature Genetics·N Tuteja, R Tuteja
Mar 21, 2007·Molecular BioSystems·Alessandro Vindigni
Feb 27, 2001·Nucleic Acids Research·A VindigniA Falaschi
Dec 31, 1997·The Journal of Biological Chemistry·A E OchemA Falaschi
Dec 9, 2000·The Journal of Biological Chemistry·R M BroshM M Seidman

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