Human ATP‐dependent RNA/DNA helicase hSuv3p interacts with the cofactor of survivin HBXIP

• Published in: The FEBS journal Vol. 272; no. 19; pp. 5008 - 5019
• Main Authors: Minczuk, Michal, Mroczek, Seweryn, Pawlak, Sebastian D., Stepien, Piotr P.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Science Ltd 01.10.2005; Blackwell Publishing Ltd
• Subjects: Adaptor Proteins, Signal Transducing; Adenosine; Adenosine Triphosphate - pharmacology; Animals; apoptosis; Binding sites; Carrier Proteins - genetics; Carrier Proteins - metabolism; Cell Line; Cell Nucleus - metabolism; Cercopithecus aethiops; Cytosol - metabolism; DEAD-box RNA Helicases; Enzyme Stability; Genetics; helicase; Hepatitis B virus; Human subjects; Humans; intracellular localization; mitochondria; Mitochondria - metabolism; Mitochondrial DNA; mitochondrial import; Protein Binding; Protein Transport; RNA Helicases - chemistry; RNA Helicases - genetics; RNA Helicases - metabolism; Two-Hybrid System Techniques
• ISSN: 1742-464X; 1742-4658
• DOI: 10.1111/j.1742-4658.2005.04910.x

The human SUV3gene encodes an NTP‐dependent DNA/RNA DExH box helicase predominantly localized in mitochondria. Its orthologue in yeast is a component of the mitochondrial degradosome complex involved in the mtRNA decay pathway. In contrast to this, the physiological function of human SUV3 remains to be elucidated. In this report we demonstrate that the hSuv3 protein interacts with HBXIP, previously identified as a cofactor of survivin in suppression of apoptosis and as a protein that binds the HBx protein encoded by the hepatitis B virus. Using deletion analysis we identified the region within the hSuv3 protein, which is responsible for binding to HBXIP. The HBXIP binding domain was found to be important for mitochondrial import and stability of the Suv3 protein in vivo. We discuss the possible involvement of the hSuv3p–HBXIP interaction in the survivin‐dependent antiapoptotic pathway.