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Lookup NU author(s): Dr Hamid Reza Soleimanpour Lichaei, Dr Joao Passos, Dr Mateusz Wydro, Dr Joanna Rorbach, Dr Richard Temperley, Professor Robert Lightowlers, Professor Zofia Chrzanowska-LightowlersORCiD
Human mitochondria contain their own genome, encoding 13 polypeptides that are synthesized within the organelle. The molecular processes that govern and facilitate this mitochondrial translation remain unclear. Many key factors have yet to be characterized-for example, those required for translation termination. All other systems have two classes of release factors that either promote codon-specific hydrolysis of peptidyl-tRNA (class I) or lack specificity but stimulate the dissociation of class I factors from the ribosome (class II). One human mitochondrial protein has been previously identified in silico as a putative member of the class I release factors. Although we could not confirm the function of this factor, we report the identification of a different mitochondrial protein, mtRF1a, that is capable in vitro and in vivo of terminating translation at UAA/UAG codons. Further, mtRF1a depletion in HeLa cells led to compromised growth in galactose and increased production of reactive oxygen species. © 2007 Elsevier Inc. All rights reserved.
Author(s): Soleimanpour-Lichaei HR, Kuhl I, Gaisne M, Passos JF, Wydro M, Rorbach J, Temperley R, Bonnefoy N, Tate W, Lightowlers R, Chrzanowska-Lightowlers Z
Publication type: Article
Publication status: Published
Journal: Molecular Cell
Year: 2007
Volume: 27
Issue: 5
Pages: 745-757
Print publication date: 01/09/2007
ISSN (print): 1097-2765
ISSN (electronic): 1097-4164
Publisher: Cell Press
URL: http://dx.doi.org/10.1016/j.molcel.2007.06.031
DOI: 10.1016/j.molcel.2007.06.031
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