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Nucleic Acids Research, 1995, Vol. 23, No. 13 2457-2463
© 1995

ENZYMOLOGY

Purification and properties of human DNA helicase VI

Narendra Tuteja, Alexander ochem, Poonam Taneja, Renu Tuteja, Doris Skopac' and Arturo Falaschi*

International Centre for Genetic Enginering and Biotechnology Padriciano 99,I-34012 Trieste, Italy

*To whom corespondence should be addressed

Received April 1, 1995. Accepted May 30, 1995.

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, llgase, topoisomerase, nicking and nuclease activities. The enzyme behaves as a monomer having an Mr of 128 kDa, whether determined with SDS-PAGE, or in native conditions. Photoaffinlty labelling wfth [{alpha}–32PJATP 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 RNARNA hybrids. HDH VI unwinds DNA unidirectionally by moving In the 3' to 5' direction along the bound strand.


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