TY - JOUR
T1 - mtRF1a Is a Human Mitochondrial Translation Release Factor Decoding the Major Termination Codons UAA and UAG
AU - Soleimanpour-Lichaei, Hamid Reza
AU - Kühl, Inge
AU - Gaisne, Mauricette
AU - Passos, Joao F.
AU - Wydro, Mateusz
AU - Rorbach, Joanna
AU - Temperley, Richard
AU - Bonnefoy, Nathalie
AU - Tate, Warren
AU - Lightowlers, Robert
AU - Chrzanowska-Lightowlers, Zofia
N1 - Funding Information:
We would like to thank Linda Spremulli (North Carolina) for providing initial constructs; P. Belenguer, G. Dujardin, T. Fox, C. Lemaire, and J. Velours for yeast strains or antibodies; L. He for assistance with the mtDNA copy number estimation; and T. Edgar for invaluable training in the release factor assays. G. Vinatier and K. Vasileiadou participated to the initial stages of the yeast work. I.K., M.G., and N.B. are supported by the Association Française contre les Myopathies and by Agence Nationale de la Recherche grant JCJC06-136672. The Iranian Government provided support (for H.R.S.-L.). J.R. and M.W. were funded by EC-MCEST (contract MEST-CT-FP6-503684). R.L. and Z.C.-L. wish to acknowledge the Wellcome Trust for continuing support.
PY - 2007/9/7
Y1 - 2007/9/7
N2 - 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.
AB - 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.
KW - RNA
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U2 - 10.1016/j.molcel.2007.06.031
DO - 10.1016/j.molcel.2007.06.031
M3 - Article
C2 - 17803939
AN - SCOPUS:34548276891
SN - 1097-2765
VL - 27
SP - 745
EP - 757
JO - Molecular Cell
JF - Molecular Cell
IS - 5
ER -