Stimulation of the DNA unwinding activity of human DNA helicase II/Ku by phosphorylation.

Abstract:

:The Ku autoantigen is a heterodimeric protein of 70- and 83-kDa subunits, endowed with duplex DNA end-binding capacity and DNA helicase activity (Human DNA Helicase II, HDH II). HDH II/Ku is well established as the DNA binding component, the regulatory subunit as well as a substrate for the DNA-dependent protein kinase DNA-PK, a complex involved in the repair of DNA double-strand breaks and in V(D)J recombination in eukaryotes. The effects of phosphorylation by this kinase on the helicase activity of Escherichia coli-produced HDH II/Ku were studied. The rate of DNA unwinding by recombinant HDH II/Ku heterodimer is stimulated at least fivefold upon phosphorylation by DNA-PK(cs). This stimulation is due to the effective transfer of phosphate residues to the helicase rather than the mere presence of the complex. In vitro dephosphorylation of HeLa cellular HDH II/Ku caused a significant decrease in the DNA helicase activity of this enzyme.

journal_name

Arch Biochem Biophys

authors

Ochem AE,Rechreche H,Skopac D,Falaschi A

doi

10.1016/j.abb.2007.11.005

subject

Has Abstract

pub_date

2008-02-01 00:00:00

pages

1-7

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(07)00540-1

journal_volume

470

pub_type

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