ArticleProceedings of the National Academy of Sciences of the United States of America2007
Crystal structure of the GINS complex and functional insights into its role in DNA replication.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 104 citations in OpenAlex.
- Archaeal and eukaryotic MCM rings sequentially melt DNA for replication initiation.Nature communications · 2026Article
- Unraveling the oncogenic and immunomodulatory roles of GINS1: a systematic pan-cancer study.Cancer cell international · 2026Article
- Integrative eQTL and Mendelian randomization analysis reveals key genes in colorectal cancer.Discover oncology · 2025Article
- HSF1 remodels mitochondrial biogenesis and function in cancer cells via TIMM17A.bioRxiv : the preprint server for biology · 2025Article
- Structure of the Saccharolobus solfataricus GINS tetramer.Acta crystallographica. Section F, Structural biology communications · 2025Article
- GINS2 promotes oral squamous cell carcinoma progression and immune evasion by recruiting PD-L1Frontiers in immunology · 2025Article
- Site directed mutagenesis reveals functional importance of conserved amino acid residues within the N-terminal domain of Dpb2 in budding yeast.Archives of microbiology · 2024Article
- TopBP1 utilises a bipartite GINS binding mode to support genome replication.Nature communications · 2024Article
- Morphological and transcriptomic responses/acclimations of erect-type submerged macrophyteEcology and evolution · 2023Article
- Infections in DNA Repair Defects.Pathogens (Basel, Switzerland) · 2023Review
- Review
- Developing mRNA signatures as a novel prognostic biomarker predicting high risk multiple myeloma.Frontiers in oncology · 2023Article
- Identification of GINS1 as a therapeutic target in the cancer patients infected with COVID-19: a bioinformatics and system biology approach.Hereditas · 2022Article
- GINS1 promotes the proliferation and migration of glioma cells through USP15-mediated deubiquitination of TOP2A.iScience · 2022Article
- Family D DNA polymerase interacts with GINS to promote CMG-helicase in the archaeal replisome.Nucleic acids research · 2022Article
- E2F1-mediated GINS2 transcriptional activation promotes tumor progression through PI3K/AKT/mTOR pathway in hepatocellular carcinoma.American journal of cancer research · 2022Article
- In silico recognition of a prognostic signature in basal-like breast cancer patients.PloS one · 2022Article
- Multiple RNA virus matrix proteins interact with SLD5 to manipulate host cell cycle.The Journal of general virology · 2021Article
- The intra-S phase checkpoint directly regulates replication elongation to preserve the integrity of stalled replisomes.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The GINS complex, which contains the four subunits Sld5, Psf1, Psf2, and Psf3, is essential for both the initiation and progression of DNA replication in eukaryotes. GINS associates with the MCM2-7 complex and Cdc45 to activate the eukaryotic minichromosome maintenance helicase. It also appears to interact with and stimulate the polymerase activities of DNA polymerase epsilon and the DNA polymerase alpha-primase complex. To further understand the functional role of GINS, we determined the crystal structure of the full-length human GINS heterotetramer. Each of the four subunits has a major domain composed of an alpha-helical bundle-like structure. With the exception of Psf1, each of the other subunits has a small domain containing a three-stranded beta-sheet core. Each full-length protein in the crystal has unstructured regions that are all located on the surface of GINS and are probably involved in its interaction with other replication factors. The four subunits contact each other mainly through alpha-helices to form a ring-like tetramer with a central pore. This pore is partially plugged by a 16-residue peptide from the Psf3 N terminus, which is unique to some eukaryotic Psf3 proteins and is not required for tetramer formation. Removal of these N-terminal 16 residues of Psf3 from the GINS tetramer increases the opening of the pore by 80%, suggesting a mechanism by which accessibility to the pore may be regulated. The structural data presented here indicate that the GINS tetramer is a highly stable complex with multiple flexible surface regions.
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