Ask about this productRelated genes to: GPN2 antibody
- Gene:
- GPN2 NIH gene
- Name:
- GPN-loop GTPase 2
- Previous symbol:
- ATPBD1B
- Synonyms:
- FLJ10349
- Chromosome:
- 1p36.11
- Locus Type:
- gene with protein product
- Date approved:
- 2005-08-12
- Date modifiied:
- 2015-08-25
Related products to: GPN2 antibody
Related articles to: GPN2 antibody
- [This corrects the article DOI: 10.1371/journal.pone.0313597.]. - Source: PubMed
Publication date: 2026/03/09
Wang LeLi PanZeng PeiXie DebaoGao MengdiMa LujieSohail AamirZeng Fanli - Prolonged defects in RNA polymerase II (RNAPII) assembly lead to the accumulation of its subunits in cytoplasmic foci, but the cellular consequences of this phenomenon remain unclear. Building on our previous discovery that GPN3 dysfunction induces reversible formation of Rpb1 foci, a process termed the RNAPII Assembly Stress Response (RASR), we examined whether RASR represents a general response to RNAPII assembly defects. Here, we show that inactivation of all three GPN proteins (Npa3/Gpn1, Gpn2, and Gpn3) results in reversible accumulation of Rpb1, Rpb2, and Rpb3 in cytoplasmic foci, establishing RASR as a conserved pathway triggered by impaired polymerase assembly. We also identify the molecular chaperone Hsp82 as a component that accumulates in these foci and partially colocalizes with them. Biochemical analyses indicate that the condensates are protein based and nucleic acid free, resist dissolution by 1,6-hexanediol, and show dynamic behavior in fluorescence recovery after photobleaching (FRAP) experiments. Transcriptomic profiling reveals coordinated regulation of ribosome biogenesis genes and metabolic pathways, including amino acid metabolism, the TCA cycle, and purine biosynthesis. Oxidative stress induced by H₂O₂ further increases foci formation, highlighting the redox sensitivity of this process. Together, these findings support a model in which RASR-induced cytoplasmic foci function as a proteostatic quality-control hub that integrates molecular chaperoning and metabolic adaptation during transcriptional stress, thereby helping to maintain the fidelity of eukaryotic gene expression. - Source: PubMed
Publication date: 2026/01/05
Wang LeXie DebaoZhao XiangdongSun XizheGao MengdiWu ZehaoLi PanZeng Fanli - Plant microbiota has received increasing attention in recent years. In particular, the microbiota associated with cereals is being extensively studied to identify bacterial strains that can promote plant health and growth. Barley is the fourth most important cereal worldwide in terms of agricultural production. Intensive barley agriculture requires the use of chemical fertilizers to compensate for nutrient deficiencies in soils and limit pathogen development. The isolation and use of bacteria that can enhance the bioavailability of soil nutrients and inhibit the development of plant pathogens could ultimately limit the use of these chemicals. In this study, we have isolated from a barley microbiota three bacterial strains belonging to the genus Streptomyces. These strains were characterized and named GPA1, GPAT2, and GPN2. - Source: PubMed
Publication date: 2025/12/07
Cheminat MargauxWaeckerle LoïcAlioua AbdelmalekCognat ValérieErhardt MathieuKoechler SandrineRoger KevinMuller DanielPflieger DavidZumsteg JulieSchaller HubertArsène-Ploetze Florence - The Gpn1, Gpn2, and Gpn3 proteins are members of the GTPase GPN family; yeast Npa3 is an orthologue of the human Gpn1 protein. These proteins play a crucial role in the nuclear accumulation of RNA polymerase II, functioning as molecular chaperones. The crystallographic structures of Npa3 reveal open and closed conformations, which are dependent on the bound guanine nucleotide (GMPPCP or GDP, respectively). The open conformation of Npa3 exhibits a hydrophobic pocket proposed to be essential for the recognition and binding of specific peptides of RNA polymerase II, contributing to its biogenesis; however, structural data on these complexes remain unavailable. In this work, we present models of the interactions between the crystallographic structure of monomeric Npa3 in its open conformation and yeast RNA polymerase II peptides, generated through flexible computational docking. To identify inhibitors of these interactions, potentially useful in understanding the molecular and cellular functions of these proteins, we performed molecular docking experiments using a designed library of FDA-approved compounds on both the Npa3 structure and a homology model of human Gpn1. Our analysis identified potential inhibitors, including atovaquone for both Npa3 and Gpn1 (docking scores: -14.4 and -13.5 kcal/mol, respectively) and tibolone for Npa3 (-13.6 kcal/mol), following flexible docking optimization. Additionally, our docking models suggest key residues in Npa3 such as F143 and W179, which may be critical for recognizing RNA polymerase II subunits and drug-like molecules. These findings can be further explored through biochemical and mutagenesis studies to assess their roles in RNA polymerase II recognition. - Source: PubMed
Publication date: 2025/09/26
Muñiz-Luna Julio ASantiago ÁngelCristóbal-Mondragón Gema RCalera Mónica RSánchez-Olea RobertoPastor Nina - Gpn2 is a highly conserved protein essential for the assembly of RNA polymerase II (RNAPII) in eukaryotic cells. Mutations in Gpn2, specifically Phe105Tyr and Leu164Pro, confer temperature sensitivity and significantly impair RNAPII assembly. Despite its crucial role, the complete range of Gpn2 functions remains to be elucidated. To further explore these functions, we conducted large-scale multicopy suppressor screening in budding yeast, aiming to identify genes whose overexpression could mitigate the growth defects of a temperature-sensitive gpn2 mutant (gpn2ts) at restrictive temperatures. We screened over 30,000 colonies harboring plasmids from a multicopy genetic library and identified 31 genes that rescued the growth defects of gpn2ts to various extents. Notably, we found that PAB1, CDC5, and RGS2 reduced the drug sensitivity of gpn2ts mutants. These findings lay a theoretical foundation for future studies on the function of Gpn2 in RNAPII assembly. - Source: PubMed
Publication date: 2024/12/06
Wang LeLi PanZeng PeiXie DebaoGao MengdiMa LujieSohail AamirZeng Fanli