Localisation of the human hSuv3p helicase in the mitochondrial matrix and its preferential unwinding of dsDNA.

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 Res

journal_title

Nucleic acids research

authors

Minczuk M,Piwowarski J,Papworth MA,Awiszus K,Schalinski S,Dziembowski A,Dmochowska A,Bartnik E,Tokatlidis K,Stepien PP,Borowski P

doi

10.1093/nar/gkf647

keywords:

subject

Has Abstract

pub_date

2002-12-01 00:00:00

pages

5074-86

issue

23

eissn

0305-1048

issn

1362-4962

journal_volume

30

pub_type

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