Ski7p G protein interacts with the exosome and the Ski complex for 3'-to-5' mRNA decay in yeast

Araki, Yasuhiro

doi:10.1093/emboj/20.17.4684

Cited by 197 publications

(207 citation statements)

References 54 publications

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“…The activity of Ski7p is of particular interest because it is a GTP-binding protein consisting of two separate domains, namely the C-terminal domain homologous to the GTP-binding elongation factor 1a (EF1a) and the N-terminal domain similar to the N domain of the GTP-binding eukaryotic releasing factor 3 (eRF3) (Araki et al, 2001). The N domain of Ski7p is required and sufficient for the 3 0 to 5 0 mRNA degradation.…”

Section: Yeast Ski Complexmentioning

confidence: 99%

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Post‐transcriptional regulation of gene expression by degradation of messenger RNAs

Bevilacqua

Ceriani

Capaccioli

et al. 2003

Journal Cellular Physiology

294

259

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Recent evidence suggests that gene expression may be regulated, at least in part, at post-transcriptional level by factors inducing the extremely rapid degradation of messenger RNAs. These factors include reactions between adenyl-uridyl-rich elements (AREs) of the relevant mRNA and either specific proteins that bind to these elements or exosomes. This review deals with examples of the proteins (AU-rich binding proteins, AUBPs) and exosomes, which have been shown to form complexes with AREs and bring about rapid degradation of the relevant mRNA, and with certain other factors, which protect the RNA from such degradation. The biochemical and physiological factors underlying the stability of messenger RNAs carrying the ARE motifs will be reviewed in the light of their emerging significance for cell physiology, human pathology, and molecular medicine. We also consider the possible application of the results of recent insights into the mechanisms to pharmacological interventions to prevent or cure disorders, especially developmental disorders, which the suppression of gene expression may bring about. Molecular targeting of specific steps in protein degradation by synthetic compounds has already been utilized for the development of pharmacological therapies.

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Section: Yeast Ski Complexmentioning

confidence: 99%

“…Two independent mechanisms of how Ski7p regulates mRNA decay have been proposed (Araki et al, 2001). The first is that Ski7p stimulates the RNA helicases and the exoribonucleases present in the Ski complex and in the exosome respectively.…”

Section: Mechanisms Of Exosome Activationmentioning

confidence: 99%

Post‐transcriptional regulation of gene expression by degradation of messenger RNAs

Bevilacqua

Ceriani

Capaccioli

et al. 2003

Journal Cellular Physiology

294

259

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“…(41/42-like heterodimer) [31] Cofactors for the exosomes without 3¢ exoRNase activity RhlB RNA helicase [50] Degradosome complex in certain bacteria [51] Ski7p and Ski RNA helicase complex [52,53] Mtr4p RNA helicase and TRAMP complex [54], Rrp47 [48], Nrd1 [55] RNA helicase associated with AU-rich element or RHAU [56], KSRP [57], TTP [58] a It is not known yet whether human nuclear and cytoplasmic exosomes contain different components.…”

Section: Chloroplastmentioning

confidence: 99%

“…Yeast cytoplasmic exosome, through the G protein Ski7p, interacts with a Ski ternary-complex consisting of the RNA helicases Ski2p, Ski3p and Ski8p [52,53]. The Ski ternary-complex is a cofactor promoting exosome 3¢ to 5¢ mRNA degradation.…”

Section: Chloroplastmentioning

confidence: 99%

The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines

2007

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The structure and function of polynucleotide phosphorylase (PNPase) and the exosome, as well as their associated RNA-helicases proteins, are described in the light of recent studies. The picture raised is of an evolutionarily conserved RNA-degradation machine which exonucleolytically degrades RNA from 3¢ to 5¢. In prokaryotes and in eukaryotic organelles, a trimeric complex of PNPase forms a circular doughnutshaped structure, in which the phosphorolysis catalytic sites are buried inside the barrel-shaped complex, while the RNA binding domains create a pore where RNA enters, reminiscent of the protein degrading complex, the proteasome. In some archaea and in the eukaryotes, several different proteins form a similar circle-shaped complex, the exosome, that is responsible for 3¢ to 5¢ exonucleolytic degradation of RNA as part of the processing, quality control, and general RNA degradation process. Both PNPase in prokaryotes and the exosome in eukaryotes are found in association with protein complexes that notably include RNA helicase.

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“…The last protein in this category is Ski8, which has at least two separable functions. In vegetative cells it is part of a multiprotein complex in the cytoplasm that is involved in degradation and translational repression of nonpolyadenylated RNA (Masison et al 1995;Jacobs Anderson and Parker 1998;van Hoof et al 2000;Araki et al 2001). During meiosis, however, Ski8 relocalizes to the nucleus and associates with meiotic chromosomes where it acts as a direct partner of Spo11 Arora et al 2004).…”

Section: Introductionmentioning

confidence: 99%

Interactions between Mei4, Rec114, and other proteins required for meiotic DNA double-strand break formation in Saccharomyces cerevisiae

et al. 2007

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In most sexually reproducing organisms, meiotic recombination is initiated by DNA double-strand breaks (DSBs) formed by the Spo11 protein. In budding yeast, nine other proteins are also required for DSB formation, but roles of these proteins and interactions among them are poorly understood. We report here further studies of the behaviors of these proteins. Consistent with other studies, we find that Mei4 and Rec114 bind to chromosomes from leptonema through early pachynema. Both proteins showed only limited colocalization with the meiotic cohesin subunit Rec8, suggesting that Mei4 and Rec114 associated preferentially with chromatin loops. Rec114 localization was independent of other DSB factors, but Mei4 localization was strongly dependent on Rec114 and Mer2. Systematic deletion analysis identified protein regions important for a previously described two-hybrid interaction between Mei4 and Rec114. We also report functional characterization of a previously misannotated 5′ coding exon of REC102. Sequences encoded in this exon are essential for DSB formation and for Rec102 interaction with Rec104, Spo11, Rec114, and Mei4. Finally, we also examined genetic requirements for a set of previously described two-hybrid interactions that can be detected only when the reporter strain is induced to enter meiosis. This analysis reveals new functional dependencies for interactions among the DSB proteins. Taken together, these studies support the view that Mei4, Rec114, and Mer2 make up a functional subgroup that is distinct from other subgroups of the DSB proteins: Spo11-Ski8, Rec102-Rec104, and Mre11-Rad50-Xrs2. These studies also suggest that an essential function of Rec102 and Rec104 is to connect Mei4 and Rec114 to Spo11.

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Ski7p G protein interacts with the exosome and the Ski complex for 3'-to-5' mRNA decay in yeast

Cited by 197 publications

References 54 publications

Post‐transcriptional regulation of gene expression by degradation of messenger RNAs

Post‐transcriptional regulation of gene expression by degradation of messenger RNAs

The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines

Interactions between Mei4, Rec114, and other proteins required for meiotic DNA double-strand break formation in Saccharomyces cerevisiae

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