RNA asymmetric distribution and daughter/mother differentiation in yeast

Darzacq, Xavier; Powrie, Erin A.; Gu, Wei; Singer, Robert H.; Zenklusen, Daniel

doi:10.1016/j.mib.2003.10.005

Cited by 44 publications

(34 citation statements)

References 45 publications

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“…Ash1 accumulates mainly in the nuclei of daughter cells because its mRNA is first moved as a translationally inactive ribonucleoprotein particle (RNP) to the daughter cell by the type V myosin Myo4 traveling on cytoplasmic actin cables and then translated as the cells divide. (Darzacq et al 2003;Paquin et al 2007;Hasegawa et al 2008;Paquin and Chartrand 2008). Ace2 localization does not require cytoskeletal components needed for Ash1 asymmetry (Weiss et al 2002).…”

Section: Regulation Of Septation Machinery and The Cytokinetic Apparatusmentioning

confidence: 99%

Mitotic Exit and Separation of Mother and Daughter Cells

2012

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Productive cell proliferation involves efficient and accurate splitting of the dividing cell into two separate entities. This orderly process reflects coordination of diverse cytological events by regulatory systems that drive the cell from mitosis into G1. In the budding yeast Saccharomyces cerevisiae, separation of mother and daughter cells involves coordinated actomyosin ring contraction and septum synthesis, followed by septum destruction. These events occur in precise and rapid sequence once chromosomes are segregated and are linked with spindle organization and mitotic progress by intricate cell cycle control machinery. Additionally, critical parts of the mother/daughter separation process are asymmetric, reflecting a form of fate specification that occurs in every cell division. This chapter describes central events of budding yeast cell separation, as well as the control pathways that integrate them and link them with the cell cycle.

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Section: Regulation Of Septation Machinery and The Cytokinetic Apparatusmentioning

confidence: 99%

Mitotic Exit and Separation of Mother and Daughter Cells

2012

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“…Most experimental evidence that mRNA molecules are unevenly distributed within the cell is from in situ fluorescent analyses (Darzacq et al, 2003). A few studies (Diehn et al, 2000;Marc et al, 2002;de Jong et al, 2006) used DNA microarrays to establish a list of genes whose mRNA is preferentially translated on membrane-bound polysomes.…”

Section: Quantitative Analysis Of Asymmetric Mrna Localizationmentioning

confidence: 99%

Mitochondria-associated Yeast mRNAs and the Biogenesis of Molecular Complexes

Garcia

Darzacq

Delaveau

et al. 2007

MBoC

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The coherence of mitochondrial biogenesis relies on spatiotemporally coordinated associations of 800 -1000 proteins mostly encoded in the nuclear genome. We report the development of new quantitative analyses to assess the role of local protein translation in the construction of molecular complexes. We used real-time PCR to determine the cellular location of 112 mRNAs involved in seven mitochondrial complexes. Five typical cases were examined by an improved FISH protocol. The proteins produced in the vicinity of mitochondria (MLR proteins) were, almost exclusively, of prokaryotic origin and are key elements of the core construction of the molecular complexes; the accessory proteins were translated on free cytoplasmic polysomes. These two classes of proteins correspond, at least as far as intermembrane space (IMS) proteins are concerned, to two different import pathways. Import of MLR proteins involves both TOM and TIM23 complexes whereas non-MLR proteins only interact with the TOM complex. Site-specific translation loci, both outside and inside mitochondria, may coordinate the construction of molecular complexes composed of both nuclearly and mitochondrially encoded subunits. INTRODUCTIONMost mitochondrial proteins of eukaryotic cells are encoded by nuclear genes and synthesized by cytoplasmic ribosomes. However, a few proteins are encoded by the mitochondrial DNA and are translated inside mitochondria by bacterialtype ribosomes. The major mitochondrial import pathway of cytoplasmically translated proteins is now well understood (Koehler, 2004;Rehling et al., 2004). Although a posttranslational mechanism for import is widely accepted, it may concern only a limited class of proteins. Indeed, it was demonstrated 30 years ago that a subclass of cytoplasmic polysomes is bound to the surface of mitochondria (Kellems et al., 1975). Subsequently, experiments in yeast and human cells have suggested a cotranslational import process for some mitochondrial proteins (Fujiki and Verner, 1993;Mukhopadhyay et al., 2004). The evolutionary history of mitochondria might elucidate this apparent discrepancy between post-and cotranslational import processes. Phylogenetic studies of the yeast mitochondrial proteome have demonstrated a composite origin. It is estimated that half or more of the genes that code for the modern mitochondrial proteome originated directly from the host nuclear genome, and the other half are of bacterial origin, a consequence of a massive transfer of genes from the endosymbiont to the host nuclear genome (Marcotte et al., 2000;Karlberg et al., 2000). This symbiotic situation required the development of protein translocation machineries (translocases) in the mitochondrial membranes (Herrmann, 2003). Possibly, the two classes of nuclear genes coding for mitochondrial products may have used the same mitochondrial import pathway. However, a recent genomewide analysis (Marc et al., 2002) suggested a strong correlation between the bacterial origin of the genes and their locus specific translation on mitochondria-l...

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“…With more than 30 mRNAs localized at the bud tip, the budding yeast Saccharomyces cerevisiae is an excellent model system for studying the mechanisms behind mRNA transport and localization Darzacq et al, 2003). One of these transcripts is the ASH1 mRNA, which is localized at the distal tip of daughter cells during late anaphase (Long et al, 1997;Takizawa et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Nuclear Shuttling of She2p Couples ASH1 mRNA Localization to its Translational Repression by Recruiting Loc1p and Puf6p

Shen

Paquin

Forget

et al. 2009

MBoC

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The transport and localization of mRNAs results in the asymmetric synthesis of specific proteins. In yeast, the nucleocytoplasmic shuttling protein She2 binds the ASH1 mRNA and targets it for localization at the bud tip by recruiting the She3p-Myo4p complex. Although the cytoplasmic role of She2p in mRNA localization is well characterized, its nuclear function is still unclear. Here, we show that She2p contains a nonclassical nuclear localization signal (NLS) that is essential for its nuclear import via the importin ␣ Srp1p. Exclusion of She2p from the nucleus by mutagenesis of its NLS leads to defective ASH1 mRNA localization and Ash1p sorting. Interestingly, these phenotypes mimic knockouts of LOC1 and PUF6, which encode for nuclear RNA-binding proteins that bind the ASH1 mRNA and control its translation. We find that She2p interacts with both Loc1p and Puf6p and that excluding She2p from the nucleus decreases this interaction. Absence of nuclear She2p disrupts the binding of Loc1p and Puf6p to the ASH1 mRNA, suggesting that nuclear import of She2p is necessary to recruit both factors to the ASH1 transcript. This study reveals that a direct coupling between localization and translation regulation factors in the nucleus is required for proper cytoplasmic localization of mRNAs.

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RNA asymmetric distribution and daughter/mother differentiation in yeast

Cited by 44 publications

References 45 publications

Mitotic Exit and Separation of Mother and Daughter Cells

Mitotic Exit and Separation of Mother and Daughter Cells

Mitochondria-associated Yeast mRNAs and the Biogenesis of Molecular Complexes

Nuclear Shuttling of She2p Couples ASH1 mRNA Localization to its Translational Repression by Recruiting Loc1p and Puf6p

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