Nucleic Acids Research, 2002, Vol. 30, No. 23 5074-5086
© 2002 Oxford University Press
Localisation of the human hSuv3p helicase in the mitochondrial matrix and its preferential unwinding of dsDNA
1 Department of Genetics, University of Warsaw, Pawinskiego 5A, 02-106 Warsaw, Poland, 2 Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5A, 02-106 Warsaw, Poland, 3 Medical Research Council, Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK, 4 Abteilung für Virologie, Bernhard-Nocht-Institut für Tropenmedizin, D-20359 Hamburg, Germany, 5 School of Biological Sciences, 2.205 Stopford Building, University of Manchester, Oxford Road, Manchester M13 9PT, UK and 6 Department of Chemistry, University of Crete and Institute of Molecular Biology and Biotechnology, Heraklion, Crete, Greece
*To whom correspondence should be addressed at Department of Genetics, University of Warsaw, Pawinskiego 5A, 02-106 Warsaw, Poland. Tel: +48 0 22 659 7072; Fax: +48 0 22 658 4754; Email: stepien{at}ibb.waw.pl
We characterised the human hSuv3p protein belonging to the family of NTPases/helicases. In yeast mitochondria the hSUV3 orthologue is a component of the degradosome complex and participates in mtRNA turnover and processing, while in Caenorhabditis elegans the hSUV3 orthologue is necessary for viability of early embryos. Using immunofluorescence analysis, an in vitro mitochondrial uptake assay and sub-fractionation of human mitochondria we show hSuv3p to be a soluble protein localised in the mitochondrial matrix. We expressed and purified recombinant hSuv3p protein from a bacterial expression system. The purified enzyme was capable of hydrolysing ATP with a Km of 41.9 µM and the activity was only modestly stimulated by polynucleotides. hSuv3p unwound partly hybridised dsRNA and dsDNA structures with a very strong preference for the latter. The presented analysis of the hSuv3p NTPase/helicase suggests that new functions of the protein have been acquired in the course of evolution.
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