Yeast Genetics and Molecular Biology 1998
College Park, Maryland
August 1998


Name: Feldmann, Heidi M.
Mailing Address: institute of biochemistry, university of munich, Feodor-Lynen-Str.25, Munich, D-81377, Germany
Email Address: fmann@lmb.uni-muenchen.de
Phone and Fax numbers: 49-89-74017 406, 49-89-74107 448

040

The yeast Ku protein is a DNA helicase

Heidi M. Feldmann Institut für Biochemie der Universität München, Feodor-Lynen-Str. 25, 81377 München, Germany Tel.: 49-89-74017 406 Fax: 49-89-74017 448 e-mail: fmann@lmb.uni-muenchen.de.
Heidi M. Feldmann
institute of biochemistry, university of munich, Feodor-Lynen-Str.25, Munich, D-81377, Germany

The human Ku heterodimer has been shown to act as the regulatory subunit of DNA-dependent protein kinase holoenzyme (DNA-PK). Different cell lines have been identified as defective in one of the DNA-PK components. Theses cells are highly sensitive to X-ray irradiation and also severely deficient in the ligation of reaction intermediates generated during V(D)J recombination. The yKu heterodimer binds specifically to ends of dsDNA and to DNA discontinuities like nicks and gaps in the DNA double helix. Recently, we have shown that yKu is involved in DNA repair and recombination. Using an in vivo plasmid rejoining assay, Boulton and Jackson could demonstrate that yKu is essential in the repair of DNA double strand breaks bearing cohesive ends. In wild type strains, this damage is repaired accurately. In yku deficient strains, deletions of up to several hundred bp occur before DNA ends can be ligated. Now, we can show that yKu acts as a DNA helicase in vitro . YKu unwinds ds DNA with overhanging ends, but cannot unwind blunt end DNA. YKu helicase proceeds in 5' - 3' direction on the bound strand. Dephosphorylation of yKu using BAP results in a dramatically decrease of helicase activity. To characterize the in vivo function of yKu helicase activity we are generating mutants of the ATP-binding motif of the p70 subunit. (Supported by the Deutsche Forschungsgemeinschaft, Wi 319/11-3 project 7)


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