In Yeast, the 3′ Untranslated Region or the Presequence of <i>ATM1</i> Is Required for the Exclusive Localization of Its mRNA to the Vicinity of Mitochondria

Corral‐Debrinski, Marisol; Blugeon, Corinne; Jacq, Claude

doi:10.1128/mcb.20.21.7881-7892.2000

Cited by 130 publications

(143 citation statements)

References 57 publications

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“…Almost half the studied mRNAs from nuclear genes encoding mitochondrial products were found to be translated in the vicinity of mitochondria. This confirms and considerably extends previous observations based on a limited number of genes (Ades and Butow, 1980;Suissa and Schatz, 1982;Corral-Debrinski et al, 2000). It has already been shown that such genomic-wide approaches can produce crucial information concerning transcripts known to encode secreted or membrane proteins present in large amounts in membrane-bound fractions (Diehn et al, 2000).…”

Section: Discussionsupporting

confidence: 77%

“…We showed previously, when studying the ATM1mRNA (Corral-Debrinski et al, 2000), that the 3′-UTR contains sufficient information to target RNA to the vicinity of mitochondria. Therefore, we investigated the in vivo RNA targeting properties of eight 3'-UTRs from mRNAs that were found to be in close vicinity to mitochondria (MLR from 84 to 98).…”

Section: In Vivo Localization Of Mrnas Of High Mlr Valuementioning

confidence: 99%

“…We have shown previously (Corral-Debrinski et al, 2000) that the yeast ATM1mRNA contains cis-acting signals, in its 5′ N-terminal region and 3′-UTR, which direct heterologous RNA molecules to the vicinity of mitochondria in vivo. mRNA scientific report targeting does not require translation of the 5′ sequence, suggesting that targeting occurs independently of translation.…”

Section: Introductionmentioning

confidence: 99%

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Genome‐wide analysis of mRNAs targeted to yeast mitochondria

et al. 2002

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It is agreed that nuclear-encoded mitochondrial proteins are post-translationally targeted to mitochondria, even if, in some cases, a co-translational phase can assist the import of precursor proteins. We used yeast DNA microarrays to analyse the mRNA populations associated with free and mitochondrion-bound polysomes. As expected, many mRNAs, known to encode mitochondrial proteins, are localized to free cytoplasmic polysomes, but many are localized to mitochondrion-bound polysomes. Furthermore, the 3′-UTR of six randomly chosen mitochondrion-bound mRNAs contains sufficient information to target, in vivo, non-translatable RNA to the vicinity of mitochondria. Interestingly, genes producing mRNAs that are targeted to mitochondria are mainly of ancient bacterial origin, whereas those producing mRNAs that are translated in the cytoplasm are mainly of eukaryotic origin. These observations, which support the recent hypotheses concerning the dual origin of the mitochondrial proteome, provide new insights into the biogenesis of mitochondria.

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Section: Discussionsupporting

confidence: 77%

Section: In Vivo Localization Of Mrnas Of High Mlr Valuementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Genome‐wide analysis of mRNAs targeted to yeast mitochondria

et al. 2002

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“…It has been reported that many mRNAs and RNA-binding proteins are localized to specific compartments, along with cytoskeletal elements, in a variety of eukaryotic cells (Jansen, 2001;Kloc et al, 2002). In S. cerevisiae, many mRNAs are localized to produce proteins in specific compartments such as the daughter cell or the mitochondria (Corral-Debrinski et al, 2000;Takizawa et al, 2000;Jansen, 2001;Kwon and Schnapp, 2001;Shepard et al, 2003). These observations suggest that individual mRNAs may be consistently transported to specific areas in the yeast cell.…”

Section: Discussionmentioning

confidence: 95%

Simultaneous yet Independent Regulation of Actin Cytoskeletal Organization and Translation Initiation by Glucose inSaccharomyces cerevisiae

Uesono

Ashe

Toh‐e

2004

MBoC

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Acute glucose deprivation rapidly but transiently depolarizes the actin cytoskeleton and inhibits translation initiation in Saccharomyces cerevisiae. Neither rapid actin depolarization nor translation inhibition upon glucose removal occurs in a reg1 disruptant, which is defective in glucose repression, or in the tpk1 w mutant, which has weak cAPK activity. In the absence of additional glucose, recovery of either actin polarization or translation initiation relies upon respiration, the Snf1p protein kinase, and the transcription factors Msn2p and Msn4p. The readdition of glucose to glucose-starved cells causes a rapid recovery of actin polarization as well as translation initiation without respiration. These results indicate that the simultaneous regulation of actin polarization and translation initiation is divided into three reactions: 1) rapid shutdown depending on Reg1p and cAPK after glucose removal, 2) slow adaptation depending on Snf1p and Msn2p/4p in the absence of glucose, and 3) rapid recovery upon readdition of glucose. On glucose removal, translation initiation is rapidly inhibited in a rom2 disruptant, which is defective in rapid actin depolarization, whereas rapid actin depolarization occurs in a pop2/caf1 disruptant, which is defective in rapid inhibition of translation initiation. Thus, translation initiation and actin polarization seem to be simultaneously but independently regulated by glucose deprivation. INTRODUCTIONThe actin cytoskeleton provides the structural basis for cell polarity in the yeast Saccharomyces cerevisiae and is organized primarily into two morphologically distinct structures: cortical patches and cables (Botstein et al., 1997). Cortical patches are discrete cytoskeletal bodies at the plasma membrane, whereas actin cables are long bundles of actin filaments that are oriented along the mother-bud axis. Both structures are polarized during the budding phase of the cell cycle. During early G1 phase, cortical patches and cables are randomly distributed. As a bud emerges, cortical patches cluster at the growing tip and cables extend from the mother cell into the bud. Near the end of bud growth, the patches and cables redistribute randomly, disrupting the asymmetric distribution of the actin cytoskeleton. At the end of mitosis, patches accumulate in and cables reorient toward the mother-bud neck in connection with cytokinesis and septum formation (Botstein et al., 1997).The actin cytoskeleton is also regulated in response to environmental stimuli. Mating pheromone causes polarization of the actin cytoskeleton toward the tip of the mating projection via the Cdc42p GTPase (Read et al., 1992;Leberer et al., 1997). In contrast, stresses such as osmotic shock, heat shock, and glucose starvation depolarize the actin cytoskeleton in budded cells as shown in Figure 1A (Novick et al., 1989;Chowdhury et al., 1992;Delley and Hall, 1999). In particular, the depolarization by heat or osmotic stress is known to be a rapid and transient reaction. A recent report has indicated that the rapid depol...

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“…Genes of ancient bacterial origin comprise a significant proportion of these mitochondrion-associated mRNAs, while genes of eukaryotic origin that encode organellar proteins generally contain presequences and seem to be primarily translated on cytoplasmic polysomes [50]. The ribosomal recruitment of mRNAs requires specific features of the 3′ untranslated region of the transcripts [51]. mRNA segregation as an alternative, co-translational route for organellar protein import has only been described in mammalian and fungal cells to date, but it seems likely that such a system will be found in plant cells as well.…”

Section: Acknowledgmentsmentioning

confidence: 99%

Plant organellar protein targeting: a traffic plan still under construction

Mackenzie

2005

Trends in Cell Biology

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It has long been understood that specific features of a protein and its corresponding import apparatus dictate the behavior of mitochondrial proteins in their intracellular targeting behavior. In plants, the process by which proteins are directed to organelles has been influenced uniquely by the introduction to the cell of plastids. Parallel functions carried out within the mitochondrion and plastid permit the sharing of proteins and emergence of mechanisms to facilitate dual-targeting of the nuclear-encoded products to both compartments. These include transcriptional and translational variations, relaxation of translation initiation controls and conditional cellular influences. Details of the dual targeting system are emerging from recent studies, and evidence of variation in protein targeting behavior across plant families and across organisms implies that the system itself is in flux. This trend towards multi-targeting enhances protein versatility across eukaryotes -one means of cellular response to developmental or environmental influence.

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In Yeast, the 3′ Untranslated Region or the Presequence of ATM1 Is Required for the Exclusive Localization of Its mRNA to the Vicinity of Mitochondria

Cited by 130 publications

References 57 publications

Genome‐wide analysis of mRNAs targeted to yeast mitochondria

Genome‐wide analysis of mRNAs targeted to yeast mitochondria

Simultaneous yet Independent Regulation of Actin Cytoskeletal Organization and Translation Initiation by Glucose inSaccharomyces cerevisiae

Plant organellar protein targeting: a traffic plan still under construction

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