Abstract:
: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 K(m) of 41.9 micro M 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.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Minczuk M,Piwowarski J,Papworth MA,Awiszus K,Schalinski S,Dziembowski A,Dmochowska A,Bartnik E,Tokatlidis K,Stepien PP,Borowski Pdoi
10.1093/nar/gkf647keywords:
subject
Has Abstractpub_date
2002-12-01 00:00:00pages
5074-86issue
23eissn
0305-1048issn
1362-4962journal_volume
30pub_type
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