Mitochondrial gene history and mRNA localization: is there a correlation?

Karlberg, E. Olof; Andersson, Siv G. E.

doi:10.1038/nrg1063

Cited by 24 publications

(24 citation statements)

References 48 publications

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“…Marc et al (2002) demonstrated that the prokaryote-derived and the eukaryote-derived mitochondrial proteins are significantly different in their MLR values such that the prokaryotederived proteins typically possess high MLR values, i.e., their mRNAs are targeted to mitochondria (Karlberg and Andersson, 2003). Proteins in the outer membrane proteome and the mitochondrial surface fraction with high MLR values were highly enriched in this conserved subclass of proteins that are residents of internal mitochondrial compartments.…”

Section: Discussionmentioning

confidence: 97%

Proteomic Analysis of the Yeast Mitochondrial Outer Membrane Reveals Accumulation of a Subclass of Preproteins

Zahedi

Sickmann

Boehm

et al. 2006

MBoC

201

180

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Mitochondria consist of four compartments-outer membrane, intermembrane space, inner membrane, and matrix-with crucial but distinct functions for numerous cellular processes. A comprehensive characterization of the proteome of an individual mitochondrial compartment has not been reported so far. We used a eukaryotic model organism, the yeast Saccharomyces cerevisiae, to determine the proteome of highly purified mitochondrial outer membranes. We obtained a coverage of ϳ85% based on the known outer membrane proteins. The proteome represents a rich source for the analysis of new functions of the outer membrane, including the yeast homologue (Hfd1/Ymr110c) of the human protein causing Sjö gren-Larsson syndrome. Surprisingly, a subclass of proteins known to reside in internal mitochondrial compartments were found in the outer membrane proteome. These seemingly mislocalized proteins included most top scorers of a recent genome-wide analysis for mRNAs that were targeted to mitochondria and coded for proteins of prokaryotic origin. Together with the enrichment of the precursor form of a matrix protein in the outer membrane, we conclude that the mitochondrial outer membrane not only contains resident proteins but also accumulates a conserved subclass of preproteins destined for internal mitochondrial compartments.

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Section: Discussionmentioning

confidence: 97%

Proteomic Analysis of the Yeast Mitochondrial Outer Membrane Reveals Accumulation of a Subclass of Preproteins

Zahedi

Sickmann

Boehm

et al. 2006

MBoC

201

180

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“…It has recently been recognized that there is yet another class of nuclearencoded mitochondrial proteins where the mRNAs are bound to mitochondria before the initiation of translation. Synthesis of these mitochondrial proteins also takes place in the vicinity of the organelle (24,25,66).…”

Section: Discussionmentioning

confidence: 99%

Heterogeneous Nuclear Ribonucleoprotein K Enhances Insulin-induced Expression of Mitochondrial UCP2 Protein

Ostrowski

Klimek-Tomczak

Mikula

et al. 2004

Journal of Biological Chemistry

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The uncoupling protein 2, UCP2, is a member of a family of inner mitochondrial membrane ion carriers involved in a host of metabolic processes. UCP2 protein is encoded by nuclear genome, but the protein is found exclusively in the mitochondria. The heterogeneous nuclear ribonucleoprotein K (hnRNPK) is an RNA-binding protein involved in many processes that compose gene expression, including mRNA processing and translation. The yeast three-hybrid screen revealed K protein bound to ucp2 mRNA through sites located in the 3 -untranslated region of the transcript. ucp2 mRNA-K protein complexes were associated with polysomecoated mitochondria. Expression of exogenous K protein augmented the insulin-induced mitochondrial level of UCP2 protein that was not accompanied by a corresponding increase in ucp2 mRNA. These results suggest the insulin stimulates translation of ucp2 mRNA in a process that involves K protein.

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“…The vast majority of mitochondrial proteins are encoded in the nucleus. The corresponding genes are of prokaryotic or eukaryotic origin, derived from ancient gene transfer between endosymbiont and host or more recently from gene duplication and divergence of host genes, respectively (Karlberg and Andersson 2003). Strikingly, mRNAs encoding mitochondrial proteins from prokaryotic origin are most often translated at mitochondriabound polysomes (Marc et al 2002;Karlberg and Andersson 2003;Margeot et al 2005).…”

Section: Mrna Traycking During Asymmetric Cell Division In S Cerevisiaementioning

confidence: 99%

mRNA trafficking in fungi

Zarnack

Feldbrügge

2007

Mol Genet Genomics

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Fungal growth depends on active transport of macromolecules along the actin and/or microtubule cytoskeleton. Thereby, molecular cargo such as proteins, lipids, and mRNAs is targeted to defined subcellular regions. Active transport and localisation of mRNAs mediate localised translation so that protein synthesis occurs where protein function is required. In Saccharomyces cerevisiae, actomyosin-dependent mRNA trafficking participates in polar growth, asymmetric cell division, targeting of membrane proteins and import of mitochondrial proteins. The best-understood example is transport of ASH1 mRNA to the distal pole of the incipient daughter cell. cis-acting RNA sequences are recognised by the RNA-binding protein She2p that is connected via the adaptor She3p to the molecular motor Myo4p. Local translation at the poles of daughter cells causes Ash1p to accumulate predominantly in nuclei of daughter cells, where this transcription factor inhibits mating-type switching. Recently, it was also shown that actomyosin-dependent ASH1 mRNA transport directs tip cell-specific gene expression in filaments of the human pathogen Candida albicans. Furthermore, in the plant pathogen Ustilago maydis microtubule-dependent shuttling of the RNA-binding protein Rrm4 is essential to determine the axis of polarity in infectious filaments. Thus, mRNA trafficking appears to be universally required for polar growth of fungi.

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Mitochondrial gene history and mRNA localization: is there a correlation?

Cited by 24 publications

References 48 publications

Proteomic Analysis of the Yeast Mitochondrial Outer Membrane Reveals Accumulation of a Subclass of Preproteins

Proteomic Analysis of the Yeast Mitochondrial Outer Membrane Reveals Accumulation of a Subclass of Preproteins

Heterogeneous Nuclear Ribonucleoprotein K Enhances Insulin-induced Expression of Mitochondrial UCP2 Protein

mRNA trafficking in fungi

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