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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao FEBS Journalarrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
FEBS Journal
Article . 2005 . Peer-reviewed
License: Wiley Online Library User Agreement
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FEBS Journal
Article . 2005
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Human ATP‐dependent RNA/DNA helicase hSuv3p interacts with the cofactor of survivin HBXIP

Authors: Sebastian D. Pawlak; Michal Minczuk; Seweryn Mroczek; Piotr P. Stepien; Piotr P. Stepien;

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

Abstract

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.

Keywords

Cell Nucleus, Cell Line, Mitochondria, DEAD-box RNA Helicases, Protein Transport, Adenosine Triphosphate, Cytosol, Two-Hybrid System Techniques, Chlorocebus aethiops, Enzyme Stability, Animals, Humans, Carrier Proteins, RNA Helicases, Adaptor Proteins, Signal Transducing, Protein Binding

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
34
Top 10%
Top 10%
Top 10%
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