ArticleGenetics2005
Association of the GTP-binding protein Gtr1p with Rpc19p, a shared subunit of RNA polymerase I and III in yeast Saccharomyces cerevisiae.
Article in Genetics, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Chemical-Genetic Interactions with the Proline Analog L-Azetidine-2-Carboxylic Acid inG3 (Bethesda, Md.) · 2020Article
- Stress granule-defective mutants deregulate stress responsive transcripts.PLoS genetics · 2014Article
- Environmental signaling through the mechanistic target of rapamycin complex 1: mTORC1 goes nuclear.Cell cycle (Georgetown, Tex.) · 2014Review
- The intrinsic GTPase activity of the Gtr1 protein from Saccharomyces cerevisiae.BMC biochemistry · 2012Article
- Article
- Amino acid regulation of TOR complex 1.American journal of physiology. Endocrinology and metabolism · 2009Review
- NOP132 is required for proper nucleolus localization of DEAD-box RNA helicase DDX47.Nucleic acids research · 2006Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Yeast Gtr1p and its human homolog RRAG A belong to the Ras-like small G-protein superfamily and genetically interact with RCC1, a guanine nucleotide exchange factor for Ran GTPase. Little is known regarding the function of Gtr1p. We performed yeast two-hybrid screening using Gtr1p as the bait to find interacting proteins. Rpc19p, a shared subunit of RNA polymerases I and III, associated with Gtr1p. The association of Gtr1p with Rpc19p occurred in a GTP-form-specific manner. RRAG A associated with RPA16 (human Rpc19p homolog) in a GTP-form-specific manner, suggesting that the association is conserved during evolution. Ribosomal RNA and tRNA synthesis were reduced in the gtr1Delta strain expressing the GDP form of Gtr1p, but not the GTP form of Gtr1p. Gel-filtration studies revealed an accumulation of the smaller Rpc19p-containing complex, but not of A135, in the gtr1Delta strain. Here, we propose that Gtr1p is involved in RNA polymerase I and III assembly by its association with Rpc19p and could be a mediator that links growth regulatory signals with ribosome biogenesis.
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