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Nucleic Acids Research, 2001, Vol. 29, No. 5 1061-1067
© 2001 Oxford University Press

Identification of human DNA helicase V with the far upstream element-binding protein

Alessandro Vindigni, Alexander Ochem, Gianluca Triolo and Arturo Falaschi*

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

The properties of human DNA helicase V (HDH V) were studied in greater detail following an improved purification procedure. From 450 g of cultured cells, <0.1 mg of pure protein was isolated. HDH V unwinds DNA unidirectionally by moving in the 3' to 5' direction along the bound strand in an ATP- and Mg2+-dependent fashion. The enzyme is not processive and can also unwind partial RNA–RNA duplexes such as HDH IV and HDH VIII. The Mr determined by SDS–PAGE (66 kDa) corresponds to that measured under native conditions, suggesting that HDH V exists as a monomer in the nucleus. Microsequencing of the purified HDH V shows that this enzyme is identical to the far upstream element-binding protein (FBP), a protein that stimulates the activity of the c-myc gene by binding specifically to the ‘FUSE’ DNA region localized upstream of its promoter. The sequence of HDH V/FBP contains RGG motifs like HDH IV/nucleolin, HDH VIII/G3BP as well as other human RNA and DNA helicases identified by other laboratories.

* To whom correspondence should be addressed. Tel: +39 040 3757303; Fax: +39 040 3757353; Email: falaschi{at}icgeb.trieste.it


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