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Binding to G-quadruplex RNA activates the mitochondrial GTPase NOA1.
Max-Planck-Institute for Heart and Lung Research, Ludwigstrasse 43, 61231 Bad Nauheim, Germany.
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2013 (engelsk)Inngår i: Biochimica et Biophysica Acta, ISSN 0006-3002, E-ISSN 1878-2434, Vol. 1833, nr 12Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

NOA1 is an evolutionary conserved, nuclear encoded GTPase essential for mitochondrial function and cellular survival. The function of NOA1 for assembly of mitochondrial ribosomes and regulation of OXPHOS activity depends on its GTPase activity, but so far no ligands have been identified that regulate the GTPase activity of NOA1. To identify nucleic acids that bind to the RNA-binding domain of NOA1 we employed SELEX (Systemic Evolution of Ligands by EXponential Enrichment) using recombinant mouse wildtype NOA1 and the GTPase mutant NOA1-K353R. We found that NOA1 binds specifically to oligonucleotides that fold into guanine tetrads (G-quadruplexes). Binding of G-quadruplex oligonucleotides stimulated the GTPase activity of NOA1 suggesting a regulatory link between G-quadruplex containing RNAs, NOA1 function and assembly of mitochondrial ribosomes.

sted, utgiver, år, opplag, sider
2013. Vol. 1833, nr 12
HSV kategori
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URN: urn:nbn:se:umu:diva-116150DOI: 10.1016/j.bbamcr.2013.07.022PubMedID: 23933583OAI: oai:DiVA.org:umu-116150DiVA, id: diva2:901604
Tilgjengelig fra: 2016-02-08 Laget: 2016-02-08 Sist oppdatert: 2018-06-07

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