A general suppressor of RNA polymerase I, II and III mutations in Saccharomyces cerevisiae

Stettler, Sophie; Chiannilkulchai, Nuchanard; Denmat, Sylvie Hermann‐Le; Lalo, Dominique; Lacroute, François; Sentenac, André; Thuriaux, Pierre

doi:10.1007/bf00281615

Cited by 86 publications

(34 citation statements)

References 66 publications

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“…These observations suggest that Ssd1p is also involved in the transcription of a certain subset of genes. In fact, SSD1-V suppresses mutations in pol I, II and III (Stettler et al 1993). Using a genome-wide approach, Ssd1p was recently shown to bind to more than 50 (Hogan et al 2008) or 150 (Jansen et al 2009) target mRNAs in vivo, including CLN2 (Hogan et al 2008); however, the functional significance of these Ssd1p ⁄ mRNA interactions has just begun to be elucidated (Jansen et al 2009).…”

Section: Discussionmentioning

confidence: 99%

Saccharomyces cerevisiae Ssd1p promotes CLN2 expression by binding to the 5′‐untranslated region of CLN2 mRNA

Ohyama

Koyamada

Kokubo³

2010

Genes to Cells

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In Saccharomyces cerevisiae, TFIID, which is composed of TATA-binding protein (TBP) and a set of TBP-associated factors (TAFs), mediates the transcription of most class II genes. Previous studies have shown that CLN2 expression was significantly reduced by taf1-ts2, but not by taf1-N568D, although both mutations display similar temperature-sensitive growth phenotypes and transcriptional defects in other genes. Here, we show that the reduced expression of CLN2 is not because of differences in taf1 alleles in the previous experiments but because of allelic differences at the SSD1 locus in the host strains. Specifically, ssd1-d reduces CLN2 expression when combined with taf1. Ssd1p expressed from SSD1-V, but not from ssd1-d, stabilizes a subpopulation of CLN2 mRNA in wild-type and taf1-N568D strains and facilitates the continuous transcription of CLN2 after heat shock in the taf1-N568D strain. Reporter assays show that both activities appear to depend on the 5¢-untranslated region of CLN2 mRNA and that Ssd1p binds to this region via its amino-and carboxy-terminal domains. Based on these observations, we propose a model for the action of Ssd1p and discuss its biologic role.

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Section: Discussionmentioning

confidence: 99%

Saccharomyces cerevisiae Ssd1p promotes CLN2 expression by binding to the 5′‐untranslated region of CLN2 mRNA

Ohyama

Koyamada

Kokubo³

2010

Genes to Cells

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“…Ssd1 is the first example of a yeast mRNP that shuttles into and out of the nucleus and has a role both in polarized mRNA localization and in translational repression. This complexity of Ssd1 function coupled with the diversity of its associated mRNAs likely account for the large variety of SSD1 genetic interactions (Sutton et al, 1991;Chiannilkulchai et al, 1992;Turcq et al, 1992;Stettler et al, 1993;Uesono et al, 1994;Tsuchiya et al, 1996;Luukkonen and Seraphin, 1999;Moriya and Isono, 1999;Kaeberlein and Guarente, 2002;Wheeler et al, 2003;Kaeberlein et al, 2004;Tanaka et al, 2007;Mir et al, 2009).…”

Section: Ssd1-like Mrna Functions In Other Organismsmentioning

confidence: 99%

Nucleocytoplasmic shuttling of Ssd1 defines the destiny of its bound mRNAs

Kurischko

Kuravi

Herbert

et al. 2011

Molecular Microbiology

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SUMMARY Mechanisms that control mRNA metabolism are critical for cell function, development and stress response. The S. cerevisiae mRNA-binding protein Ssd1 has been implicated in mRNA processing, aging, stress response and maintenance of cell integrity. Ssd1 is a substrate of the LATS/NDR tumor suppressor orthologue Cbk1 kinase. Previous data indicate that Ssd1 localizes to the cytoplasm, however biochemical interactions suggest that Ssd1 at least transiently localizes to the nucleus. We therefore explored whether nuclear localization is important for Ssd1 cytoplasmic functions. We identified a functional NLS in the N-terminal domain of Ssd1. An Ssd1 derived NLS-GFP fusion protein and several C-terminally truncated Ssd1 proteins, which presumably lack nuclear export sequences, accumulate in the nucleus. Alanine substitution of the Ssd1 NLS prevents Ssd1 nuclear entry, mRNA binding and disrupts Srl1 mRNA localization. Moreover, Ssd1-NLS mutations abolish Ssd1 toxicity in the absence of Cbk1 phosphorylation and cause Ssd1 to localize prominently to cytoplasmic puncta. These data indicate that nuclear shuttling is critical for Ssd1 mRNA binding and Ssd1-mRNA localization in the cytoplasm. Collectively these data support the model that Ssd1 functions analogously to hnRNPs, which bind mRNA co-transcriptionally, are exported to the cytoplasm and target mRNAs to sites of localized translation and P-bodies.

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“…The fhll-A::HIS3 MW666 strain was transformed with a genomic library obtained by partial Sau3AI digestion of Saccharomyces cerevisiae DNA (strain FL100) cloned into pFL44L (Stettler et al, 1993). Ura+ transformants were selected at 25°C on Casa plates supplemented with adenine and tryptophan.…”

Section: Isolation Of Multicopy Suppressorsmentioning

confidence: 99%

“…The .fiEI-A::HIS3 strain MW666 grows very slowly and forms minute colonies at 25°C. Circa lo4 transformants were selected on uracil omission medium after transformation with a genomic library of S. cerevisiae borne on the multicopy vector pFL44L (Stettler et al, 1993). Twelve of them produced large colonies at 25°C.…”

Section: Cloning Of Ifhmentioning

confidence: 99%

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The IFH1 gene product interacts with a fork head protein in Saccharomyces cerevisiae

Chérel

Thuriaux

1995

Yeast

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FHL1 encodes a polypeptide closely related to the fork head protein family of transcriptional activators. Deleting this gene leads to a slow-growth phenotype with impaired rRNA maturation. IFH1 (located on chromosome IV) was isolated as a dosage-dependent suppressor partially correcting the growth defect of the fhl1 deletion. It codes for a highly hydrophilic protein with a predicted molecular weight of 122 kDa and a pI of 4.8, that is very rich in charged residues (mostly acidic) but otherwise unrelated to any known protein. Carboxy-terminal deletions removing the last third of the protein lead to a leaky growth phenotype with impaired rRNA maturation, as in the case of the fhl1 deletion. A full deletion of IFH1 is lethal, but growth was restored in a strain deleted for both IFH1 and FHL1. Thus, Ifh1p is essential for growth, but only in the presence of a functional Fhp1p protein. Conversely, its overexpression by increased gene dosage partially compensates for the genetic inactivation of Fhl1p. These data suggest a direct interaction between the Fhl1p and Ifh1p proteins, and are consistent with a model where Fhl1p is converted from a transcriptional repressor to an activator on binding of Ifh1p.

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A general suppressor of RNA polymerase I, II and III mutations in Saccharomyces cerevisiae

Cited by 86 publications

References 66 publications

Saccharomyces cerevisiae Ssd1p promotes CLN2 expression by binding to the 5′‐untranslated region of CLN2 mRNA

Saccharomyces cerevisiae Ssd1p promotes CLN2 expression by binding to the 5′‐untranslated region of CLN2 mRNA

Nucleocytoplasmic shuttling of Ssd1 defines the destiny of its bound mRNAs

The IFH1 gene product interacts with a fork head protein in Saccharomyces cerevisiae

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