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      Mitochondrial presequence and open reading frame mediate asymmetric localization of messenger RNA

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          Mitochondrial presequence and open reading frame mediate asymmetric localization of messenger RNA

          Some mRNAs of nuclear encoded mitochondrial proteins are localized asymmetrically in the vicinity of mitochondria. The Jacq laboratory now demonstrates that both the mitochondrial targeting sequence and the translation of two elements in the ORF are required for perimitochondrial localization of the ATP2 mRNA. These results link asymmetric mRNA localization with cotranslational mitochondrial protein import.

          Abstract

          Although a considerable amount of data have been gathered on mitochondrial translocases, which control the import of a large number of nuclear-encoded proteins, the preceding steps taking place in the cytosol are poorly characterized. The localization of messenger RNAs (mRNAs) on the surface of mitochondria was recently shown to involve specific classes of protein and could be an important regulatory step. By using an improved statistical fluorescent in situ hybridization technique, we analysed the elements of the ATP2 open reading frame that control its mRNA asymmetric localization. The amino-terminal mitochondrial targeting peptide (MTS) and translation of two elements in the coding sequence, R1 and R2, were required for anchoring of ATP2 mRNA to mitochondria. Unexpectedly, any MTS can replace ATP2 MTS, whereas R1 and R2 are specifically required to maintain perimitochondrial mRNA localization. These data connect the well-known MTS–translocase interaction step with a site-specific translation step and offer a mechanistic description for a co-translational import process.

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          Improved method for high efficiency transformation of intact yeast cells.

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            Translocation of proteins into mitochondria.

            About 10% to 15% of the nuclear genes of eukaryotic organisms encode mitochondrial proteins. These proteins are synthesized in the cytosol and recognized by receptors on the surface of mitochondria. Translocases in the outer and inner membrane of mitochondria mediate the import and intramitochondrial sorting of these proteins; ATP and the membrane potential are used as energy sources. Chaperones and auxiliary factors assist in the folding and assembly of mitochondrial proteins into their native, three-dimensional structures. This review summarizes the present knowledge on the import and sorting of mitochondrial precursor proteins, with a special emphasis on unresolved questions and topics of current research.
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              Global analysis of mRNA localization reveals a prominent role in organizing cellular architecture and function.

              Although subcellular mRNA trafficking has been demonstrated as a mechanism to control protein distribution, it is generally believed that most protein localization occurs subsequent to translation. To address this point, we developed and employed a high-resolution fluorescent in situ hybridization procedure to comprehensively evaluate mRNA localization dynamics during early Drosophila embryogenesis. Surprisingly, of the 3370 genes analyzed, 71% of those expressed encode subcellularly localized mRNAs. Dozens of new and striking localization patterns were observed, implying an equivalent variety of localization mechanisms. Tight correlations between mRNA distribution and subsequent protein localization and function, indicate major roles for mRNA localization in nucleating localized cellular machineries. A searchable web resource documenting mRNA expression and localization dynamics has been established and will serve as an invaluable tool for dissecting localization mechanisms and for predicting gene functions and interactions.
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                Author and article information

                Journal
                EMBO Rep
                EMBO Reports
                Nature Publishing Group
                1469-221X
                1469-3178
                April 2010
                12 March 2010
                12 March 2010
                : 11
                : 4
                : 285-291
                Affiliations
                [1 ]Laboratoire de Génétique Moléculaire, Ecole Normale Supérieure , 46 rue d'Ulm, Paris 75230, France
                Author notes
                [a ]Tel: +33 1 4432 3546; Fax: +33 1 4432 3547; E-mail: claude.jacq@ 123456ens.fr
                Article
                embor201017
                10.1038/embor.2010.17
                2854591
                20224577
                381cb081-ccea-4a46-a3fe-42753c81387b
                Copyright © 2010, European Molecular Biology Organization

                This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits distribution, and reproduction in any medium, provided the original author and source are credited. This license does not permit commercial exploitation without specific permission.

                History
                : 10 June 2009
                : 20 January 2010
                : 22 January 2010
                Categories
                Scientific Reports

                Molecular biology
                co-translational import,mitochondria,membrane-bound ribosome
                Molecular biology
                co-translational import, mitochondria, membrane-bound ribosome

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