ArticleCell cycle (Georgetown, Tex.)2013
Eukaryotic GPN-loop GTPases paralogs use a dimeric assembly reminiscent of archeal GPN.
Article in Cell cycle (Georgetown, Tex.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Structure of cytoplasmic RNA polymerase II.Nature communications · 2026Article
- Proposal of Chemical Inhibitors That Compete with the Binding of RNA Polymerase II Subunits to Essential GTPases GPN Npa3 and Gpn1.ACS omega · 2025Article
- Synthetic negative genome screen of the GPN-loop GTPase NPA3 in Saccharomyces cerevisiae.Current genetics · 2022Article
- A nuclear proteome localization screen reveals the exquisite specificity of Gpn2 in RNA polymerase biogenesis.Cell cycle (Georgetown, Tex.) · 2021Article
- Biogenesis of RNA Polymerases in Yeast.Frontiers in molecular biosciences · 2021Review
- The Phosphatase PP2A Interacts With ArnA and ArnB to Regulate the Oligomeric State and the Stability of the ArnA/B Complex.Frontiers in microbiology · 2020Article
- Gpn3 Is Essential for Cell Proliferation of Breast Cancer Cells Independent of Their Malignancy Degree.Technology in cancer research & treatment · 2019Article
- Gpn2 and Rba50 Directly Participate in the Assembly of the Rpb3 Subcomplex in the Biogenesis of RNA Polymerase II.Molecular and cellular biology · 2018Article
- Structure of GPN-Loop GTPase Npa3 and Implications for RNA Polymerase II Assembly.Molecular and cellular biology · 2015Article
- A multi-host approach for the systematic analysis of virulence factors in Cryptococcus neoformans.The Journal of infectious diseases · 2015Article
- The interactome of the atypical phosphatase Rtr1 in Saccharomyces cerevisiae.Molecular bioSystems · 2014Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GTPases are molecular switches that regulate a wide-range of cellular processes. The GPN-loop GTPase (GPN) is a sub-family of P-loop NTPase that evolved from a single gene copy in archaea to triplicate paralog genes in eukaryotes, each having a non-redundant essential function in cell. In Saccharomyces cerevisiae, yGPN1 and yGPN2 are involved in sister chromatid cohesion mechanism, whereas nothing is known regarding yGPN3 function. Previous high-throughput experiments suggested that GPN paralogs interaction may occur. In this work, GPN|GPN contact was analyzed in details using TAP-Tag approach, yeast two-hybrid assay, in silico energy computation and site-directed mutagenesis of a conserved Glu residue located at the center of the interaction interface. It is demonstrated that this residue is essential for cell viability. A chromatid cohesion assay revealed that, like yGPN1 and yGPN2, yGPN3 also plays a role in sister chromatid cohesion. These results suggest that all three GPN proteins act at the molecular level in sister chromatid cohesion mechanism as a GPN|GPN complex reminiscent of the homodimeric structure of PAB0955, an archaeal member of GPN-loop GTPase.
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