C-Terminal Truncations of the Yeast Nucleoporin Nup145p Produce a Rapid Temperature-Conditional mRNA Export Defect and Alterations to Nuclear Structure

Dockendorff, Thomas C.; Heath, Catherine V.; Goldstein, Alan L.; Snay, C A; Cole, Charles N.

doi:10.1128/mcb.17.2.906

Cited by 46 publications

(43 citation statements)

References 50 publications

(98 reference statements)

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“…Such a phenotype has previously been reported for other individual mRNA export-deficient strains (Kadowaki et al 1994b;Dockendorff et al 1997;Rout et al 2000), and we therefore decided to examine this in general by conducting Nop1p staining of all 15 deletion mutants subjected to a 42°C heat shock for 20 or 40 min. In the more severe cases (e.g., the Dmft1, Drip1, and Dsac3 strains), Nop1p fragmentation was evident in a fraction of the cells already at the 20-min time point and in all cells after 40 min of incubation at 42°C (Fig.…”

Section: Resultsmentioning

confidence: 99%

General, rapid, and transcription-dependent fragmentation of nucleolar antigens in S. cerevisiae mRNA export mutants

Thomsen

Saguez²,

Nasser³

et al. 2008

RNA

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In the yeast Saccharomyces cerevisiae, mutation of some effectors of mRNA nuclear export leads to the rapid accumulation of HSP104 RNA in transcription site-associated foci. We have screened the S. cerevisiae complement of viable gene deletion mutants for their inability to export HSP104 RNA. The 15 strains identified comprise deletions of components of the THO, Thp1p/Sac3p, and nuclear pore complexes. In all three mutant classes, retained RNA overlaps the HSP104 transcription site. Thus, an early block to HSP104 RNA export is general. Incubation of the identified deletion strains, as well as seven additional mutants, under conditions where mRNA export is blocked results in rapid dissipation of nucleolar protein and RNA constituents. Time course experiments show that dissipation of nucleolar antigens succeeds mRNA retention and is reversed when the load of nuclear mRNA ceases. Consistent with a causal role of excess nuclear mRNA, nucleolar morphology in an mRNA export mutant environment remains intact when transcription by RNA polymerase II is inhibited.

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Section: Resultsmentioning

confidence: 99%

General, rapid, and transcription-dependent fragmentation of nucleolar antigens in S. cerevisiae mRNA export mutants

Thomsen

Saguez²,

Nasser³

et al. 2008

RNA

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“…Proteolytic cleavage of a 186-kD precursor protein yields both Nup96 and Nup98 (Fontoura et al, 1999). The yeast Nup96 homolog, C-Nup145p, is also produced through proteolytic cleavage of a precursor protein that yields both C-Nup145p and N-Nup145p, the Nup98 equivalent in yeast (Dockendorff et al, 1997;Emtage et al, 1997;Teixeira et al, 1997). Database searches revealed that MOS3 is the only Nup96 homolog and the message for MOS3 only encodes AtNup96.…”

Section: Es4326 Growth Of Psm Es4326 In Mos3-1 and Mos3-2 Ismentioning

confidence: 99%

A Putative Nucleoporin 96 Is Required for Both Basal Defense and Constitutive Resistance Responses Mediated bysuppressor of npr1-1,constitutive 1

2005

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The Arabidopsis thaliana suppressor of npr1-1, constitutive 1 (snc1) mutant contains a gain-of-function mutation in a Toll Interleukin1 receptor-nucleotide binding-Leu-rich repeat–type resistance gene (R-gene), which leads to constitutive activation of disease resistance response against pathogens. In a screen for suppressors of snc1, a recessive mutation, designated mos3 (for modifier of snc1,3), was found to suppress the constitutive pathogenesis-related gene expression and resistance to virulent Pseudomonas syringae maculicola ES4326 and Peronospora parasitica Noco2 in snc1. In addition, mos3 is also compromised in resistance mediated by Resistance to Peronospora parasitica 4 (RPP4), Resistance to Pseudomonas syringae pv maculicola (RPM1), and Resistance to Pseudomonas syringae 4 (RPS4). Single mutant mos3 plants exhibited enhanced disease susceptibility to P. s. pv maculicola ES4326, suggesting that MOS3 is required for basal resistance to pathogens as well. mos3-1 was identified by map-based cloning, and it encodes a protein with high sequence similarity to human nucleoporin 96. Localization of the MOS3-green fluorescent protein fusion to the nuclear envelope further indicates that MOS3 may encode a nucleoporin, suggesting that nuclear and cytoplasmic trafficking plays an important role in both R-gene–mediated and basal disease resistance.

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“…When detected by in situ hybridization using oligo dT probes, minimal poly(A) + signal is present within the nucleus. In screening for nuclear poly(A) + RNA retention using temperature-sensitive mutants as well as single gene deletion strains, initial studies identified many genes involved in mRNA export (Gorsch et al 1995;Heath et al 1995;Li et al 1995;Saavedra et al 1996;Dockendorff et al 1997). For the essential genes identified by nuclear poly(A) + retention, the lethal phenotype was thought to be caused by a general defect of mRNA export.…”

Section: Introductionmentioning

confidence: 99%

A nucleoporin, Nup60p, affects the nuclear and cytoplasmic localization of ASH1 mRNA in S. cerevisiae

Powrie

Zenklusen

Singer³

2010

RNA

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The biogenesis of a localization-competent mRNP begins in the nucleus. It is thought that the coordinated action of nuclear and cytoplasmic components of the localization machinery is required for the efficient export and subsequent subcellular localization of these mRNAs in the cytoplasm. Using quantitative poly(A)+ and transcript-specific fluorescent in situ hybridization, we analyzed different nonessential nucleoporins and nuclear pore-associated proteins for their potential role in mRNA export and localization. We found that Nup60p, a nuclear pore protein located on the nucleoplasmic side of the nuclear pore complex, was required for the mRNA localization pathway. In a Dnup60 background, localized mRNAs were preferentially retained within the nucleus compared to nonlocalized transcripts. However, the export block was only partial and some transcripts could still reach the cytoplasm. Importantly, downstream processes were also affected. Localization of ASH1 and IST2 mRNAs to the bud was impaired in the Dnup60 background, suggesting that the assembly of a localization competent mRNP (''locasome'') was inhibited when NUP60 was deleted. These results demonstrate transcript specificity of a nuclear mRNA retention defect and identify a specific nucleoporin as a functional component of the localization pathway in budding yeast.

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C-Terminal Truncations of the Yeast Nucleoporin Nup145p Produce a Rapid Temperature-Conditional mRNA Export Defect and Alterations to Nuclear Structure

Cited by 46 publications

References 50 publications

General, rapid, and transcription-dependent fragmentation of nucleolar antigens in S. cerevisiae mRNA export mutants

General, rapid, and transcription-dependent fragmentation of nucleolar antigens in S. cerevisiae mRNA export mutants

A Putative Nucleoporin 96 Is Required for Both Basal Defense and Constitutive Resistance Responses Mediated bysuppressor of npr1-1,constitutive 1

A nucleoporin, Nup60p, affects the nuclear and cytoplasmic localization of ASH1 mRNA in S. cerevisiae

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