tailieunhanh - Báo cáo khoa học: The Cockayne syndrome group B protein is a functional dimer

Cockayne syndrome (CS) is a rare inherited human genetic disorder char-acterized by developmental abnormalities, UV sensitivity, and premature aging. The CS group B (CSB) protein belongs to the SNF2-family of DNA-dependent ATPases and is implicated in transcription elongation, transcription coupled repair, and base excision repair. It is a DNA stimula-ted ATPase and remodels chromatin in vitro. We demonstrate for the first time that full-length CSB positively cooperates in ATP hydrolysis as a function of protein concentration | iFEBS Journal The Cockayne syndrome group B protein is a functional dimer Mette Christiansen1 Tina Thorslund1 Bjarne Jochimsen2 Vilhelm A. Bohr3 and Tinna Stevnsner1 1 Danish Centre for Molecular Gerontology Department of Molecular Biology University of Aarhus Denmark 2 Department of Molecular Biology University of Aarhus Denmark 3 Laboratory of Molecular Gerontology NationalInstitute on Aging NationalInstitutes of Health Baltimore MD USA Keywords Cockayne syndrome group B protein DNA-dependent ATPase homodimer SWI2 SNF2 transcription coupled repair Correspondence T. Stevnsner Danish Centre for Molecular Gerontology Department of Molecular Biology University of Aarhus Build. 130 DK-8000 Aarhus C Denmark Tel 45 89422657 Fax 45 89422650 E-mail tvs@ Received 13 May 2005 revised 1 July 2005 accepted 4 July 2005 doi Cockayne syndrome CS is a rare inherited human genetic disorder characterized by developmental abnormalities UV sensitivity and premature aging. The CS group B CSB protein belongs to the SNF2-family of DNA-dependent ATPases and is implicated in transcription elongation transcription coupled repair and base excision repair. It is a DNA stimulated ATPase and remodels chromatin in vitro. We demonstrate for the first time that full-length CSB positively cooperates in ATP hydrolysis as a function of protein concentration. We have investigated the quaternary structure of CSB using a combination of protein-protein complex trapping experiments and gel filtration and found that CSB forms a dimer in solution. Chromatography studies revealed that enzymatically active CSB has an apparent molecular mass of approximately 360 kDa consistent with dimerization of CSB. Importantly in vivo protein cross-linking showed the presence of the CSB dimer in the nucleus of HeLa cells. We further show that dimerization occurs through the central ATPase domain of the protein. These results have implications for the mechanism of action of CSB and

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