Expression and Localization Studies of hSDA, the Human Ortholog of the Yeast SDA1 Gene

Babbio, Federica; Farinacci, Maura; Saracino, Francesca; Carbone, Maria Louisa Agostoni; Privitera, Enrica

doi:10.4161/cc.3.4.792

Cited by 11 publications

(14 citation statements)

References 17 publications

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“…The 7S and 6S pre-rRNAs and the 25S, 5.8S and 5S rRNAs were efficiently co-precipitated with Sda1-TAP. These results are consistent with reports that Sda1p localizes to the nucleolus and nucleoplasm (Buscemi et al, 2000;Babbio et al, 2004), since 7S pre-rRNA is predominantly nucleolar, whereas the final maturation of 25S and 5.8S rRNA occurs in the nucleoplasm. This suggests that Sda1p associates with 60S pre-ribosomes during late nucleolar maturation steps and accompanies them into the nucleoplasm.…”

Section: Sda1p Is a Component Of Late 60s Pre-ribosomessupporting

confidence: 93%

Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar region of Saccharomyces cerevisiae

Dez¹,

Houseley²,

Tollervey

2006

EMBO J

121

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We previously hypothesized that HEAT-repeat (Huntington, elongation A subunit, TOR) ribosome synthesis factors function in ribosome export. We report that the HEAT-repeat protein Sda1p is a component of late 60S pre-ribosomes and is required for nuclear export of both ribosomal subunits. In strains carrying the ts-lethal sda1-2 mutation, pre-60S particles were rapidly degraded following transfer to 371C. Polyadenylated forms of the 27S pre-rRNA and the 25S rRNA were detected, suggesting the involvement of the Trf4p/Air/Mtr4p polyadenylation complex (TRAMP). The absence of Trf4p suppressed polyadenylation and stabilized the pre-rRNA and rRNA. The absence of the nuclear exosome component Rrp6p also conferred RNA stabilization, with some hyperadenylation. We conclude that the nuclear-restricted pre-ribosomes are polyadenylated by TRAMP and degraded by the exosome. In sda1-2 strains at 371C, pre-40S and pre-60S ribosomes initially accumulated in the nucleoplasm, but then strongly concentrated in a subnucleolar focus, together with exosome and TRAMP components. Localization of pre-ribosomes to this focus was lost in sda1-2 strains lacking Trf4p or Rrp6p. We designate this nucleolar focus the No-body and propose that it represents a site of pre-ribosome surveillance.

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Section: Sda1p Is a Component Of Late 60s Pre-ribosomessupporting

confidence: 93%

Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar region of Saccharomyces cerevisiae

Dez¹,

Houseley²,

Tollervey

2006

EMBO J

121

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“…Thus, PcSDA 1 is probably correctly identified as the orthologue of the yeast and human SDA 1 genes. PcSDA 1 contains three putative nuclear localization signals and an acidic region in the C‐terminus, which is consistent with SDA1 in a wide range of eukaryotic organisms (Andersen et al ., ; Babbio et al ., ; Bi et al ., ; Buscemi et al ., ). PcSDA 1 was expressed most strongly in hyphae, developing sporangia and germinating cysts, and in later infection stages of P. capsici , consistent with an important role in each of these life stages.…”

Section: Discussionmentioning

confidence: 98%

“…Management of the cytoskeleton and the cell division cycle are key mechanisms required to address these challenges. Thus, the SDA1 protein, which has been identified in S. cerevisiae (Buscemi et al ., ) and human cells (Babbio et al ., ) as an important regulator of the actin cytoskeleton and also of the cell division cycle, is potentially a key player in the regulation of the growth and morphology of filamentous organisms, such as fungi (Berepiki et al ., ; Suei and Garrill, ) and oomycetes (Ketelaar et al ., ; Meijer et al ., ). However, to date, there have been no studies of this protein outside S. cerevisiae and human cells.…”

Section: Discussionmentioning

confidence: 99%

“…Accordingly, SDA 1 has been reported to be involved in mitosis and nuclear division (Adams et al ., ), and in cell proliferation (Pardee, ; Planas‐Silva and Weinberg, ; Zimmerman and Kellogg, ). In yeast, SDA1 associates with protein complexes involved in RNA metabolism (Gavin et al ., ), and might function as a trans‐acting factor in rRNA processing (Ihmels et al ., ), ribosome biogenesis (Babbio et al ., ; Fromont‐Racine et al ., ; Nissan et al ., ; Takahashi et al ., ) and protein synthesis (Zimmerman and Kellog, ). SDA1 is localized not only in the nucleolus, but also at low levels in the nucleoplasm (Andersen et al ., ; Buscemi et al ., ), which is consistent with its involvement in early to intermediate steps of ribosome biogenesis (Babbio et al ., ).…”

Section: Introductionmentioning

confidence: 99%

“…In yeast, SDA1 associates with protein complexes involved in RNA metabolism (Gavin et al ., ), and might function as a trans‐acting factor in rRNA processing (Ihmels et al ., ), ribosome biogenesis (Babbio et al ., ; Fromont‐Racine et al ., ; Nissan et al ., ; Takahashi et al ., ) and protein synthesis (Zimmerman and Kellog, ). SDA1 is localized not only in the nucleolus, but also at low levels in the nucleoplasm (Andersen et al ., ; Buscemi et al ., ), which is consistent with its involvement in early to intermediate steps of ribosome biogenesis (Babbio et al ., ). Despite its extensive characterization in S. cerevisiae and human cells, no orthologues have been characterized in filamentous fungi or oomycetes, where the filamentous polynucleate nature of the organisms creates unique challenges for the regulation of the cytoskeleton and nuclear division.…”

Section: Introductionmentioning

confidence: 99%

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Phytophthora capsici homologue of the cell cycle regulator SDA1 is required for sporangial morphology, mycelial growth and plant infection

Zhu

Yang

et al. 2015

Molecular Plant Pathology

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SDA1 encodes a highly conserved protein that is widely distributed in eukaryotic organisms. SDA1 is essential for cell cycle progression and organization of the actin cytoskeleton in yeasts and humans. In this study, we identified a Phytophthora capsici orthologue of yeast SDA1, named PcSDA1. In P. capsici, PcSDA1 is strongly expressed in three asexual developmental states (mycelium, sporangia and germinating cysts), as well as late in infection. Silencing or overexpression of PcSDA1 in P. capsici transformants affected the growth of hyphae and sporangiophores, sporangial development, cyst germination and zoospore release. Phalloidin staining confirmed that PcSDA1 is required for organization of the actin cytoskeleton. Moreover, 4',6-diamidino-2-phenylindole (DAPI) staining and PcSDA1-green fluorescent protein (GFP) fusions revealed that PcSDA1 is involved in the regulation of nuclear distribution in hyphae and sporangia. Both silenced and overexpression transformants showed severely diminished virulence. Thus, our results suggest that PcSDA1 plays a similar role in the regulation of the actin cytoskeleton and nuclear division in this filamentous organism as in non-filamentous yeasts and human cells.

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Alterations in ribosome biogenesis cause specific defects in C. elegans hermaphrodite gonadogenesis

Voutev

Killian

Ahn

et al. 2006

Developmental Biology

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Ribosome biogenesis is a cell-essential process that influences cell growth, proliferation, and differentiation. How ribosome biogenesis impacts development, however, is poorly understood. Here, we establish a link between ribosome biogenesis and gonadogenesis in Caenorhabditis elegans that affects germline proliferation and patterning. Previously, we determined that pro-1(+)activity is required in the soma--specifically, the sheath/spermatheca sublineage--to promote normal proliferation and prevent germline tumor formation. Here, we report that PRO-1, like its yeast ortholog IPI3, influences rRNA processing. pro-1 tumors are suppressed by mutations in ncl-1 or lin-35/Rb, both of which elevate pre-rRNA levels. Thus, in this context, lin-35/Rb acts as a soma-autonomous germline tumor promoter. We further report the characterization of two additional genes identified for their germline tumor phenotype, pro-2 and pro-3, and find that they, too, encode orthologs of proteins involved in ribosome biogenesis in yeast (NOC2 and SDA1, respectively). Finally, we demonstrate that depletion of additional C. elegans orthologs of yeast ribosome biogenesis factors display phenotypes similar to depletion of progenes. We conclude that the C. elegans distal sheath is particularly sensitive to alterations in ribosome biogenesis and that ribosome biogenesis defects in one tissue can non-autonomously influence proliferation in an adjacent tissue.

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Expression and Localization Studies of hSDA, the Human Ortholog of the Yeast SDA1 Gene

Cited by 11 publications

References 17 publications

Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar region of Saccharomyces cerevisiae

Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar region of Saccharomyces cerevisiae

Phytophthora capsici homologue of the cell cycle regulator SDA1 is required for sporangial morphology, mycelial growth and plant infection

Alterations in ribosome biogenesis cause specific defects in C. elegans hermaphrodite gonadogenesis

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