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Nucleic Acids Research, 2003, Vol. 31, No. 3 963-973
© 2003 Oxford University Press

Functional consequences of mutations in the conserved SF2 motifs and post-translational phosphorylation of the CSB protein

Mette Christiansen, Tinna Stevnsner, Charlotte Modin1, Pia M. Martensen1, Robert M. Brosh Jr2 and Vilhelm A. Bohr*,2

Danish Center for Molecular Gerontology and 1 Department of Molecular Biology, University of Aarhus, DK-8000 Aarhus C, Denmark and 2 Laboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, 5600 Nathan Shock Drive, Baltimore, MD 21224, USA

*To whom correspondence should be addressed. Tel: +1 410 558 8562; Fax: +1 410 558 8157; Email: vbohr{at}nih.gov

The rare inherited human genetic disorder Cockayne syndrome (CS) is characterized by developmental abnormalities, UV sensitivity and premature aging. The cellular and molecular phenotypes of CS include increased sensitivity to UV-induced and oxidative DNA lesions. Two genes are involved: CSA and CSB. The CS group B (CSB) protein has roles in transcription, transcription-coupled repair, and base excision repair. It is a DNA stimulated ATPase and remodels chromatin in vitro. Here, we have analyzed wild-type (wt) and motif II, V and VI mutant CSB proteins. We find that the mutant proteins display different degrees of ATPase activity deficiency, and in contrast to the in vivo complementation studies, the motif II mutant is more defective than motif V and VI CSB mutants. Furthermore, CSB wt ATPase activity was studied with different biologically important DNA cofactors: DNA with different secondary structures and damaged DNA. The results indicate that the state of DNA secondary structure affects the level of CSB ATPase activity. We find that the CSB protein is phosphorylated in untreated cells and that UV irradiation leads to its dephosphorylation. Importantly, dephosphorylation of the protein in vitro results in increased ATPase activity of the protein, suggesting that the activity of the CSB protein is subject to phosphorylation control in vivo. These observations may have significant implications for the function of CSB in vivo.


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