Fig 1: The structural consequences of the Gins2L52P mutation in the zebrafish GINS complex. (A) In silico generated model of the MCM-Cdc45-GINS-Ctf4 complex built using structures 3jc5 (Yuan et al., 2016), 4c8h (Simon et al., 2014), and the homology model of the zebrafish GINS complex created in this study. The MCM hexamer (cyan), Cdc45 (green), and the Ctf14 homotrimer (purple, red, and orange) are shown as surfaces, while GINS as a ribbon diagram (Gins1: yellow, Gins2: green, Gins3: red, Gins4: blue). (B) Superposition of the most populated cluster mid-structures (accounting for >90% of all structures of the equilibrium trajectory). Coloring of the Gins monomers is the same as before, darker shades are used for the wildtype, the lighter for the mutant structures (residue 52 of Gins2 shown in space-filling representation). (C) Detailed view of the site of the mutation, with a typical H-bonding motif also illustrated.
Fig 2: Gins1 deficient and Gins1, Gins2 double-deficient embryos show comparable cell death phenotypes in eyes and tecta. (A,B) The gins1elu11 frameshift allele created through genome editing shows retinal and tectal apoptosis at 2 dpf, similar to other CMG mutants. (C) Sanger sequencing of gins1elu11/elu11 embryos shows the presence of the homozygous c.250_251delCT mutation. (D,E) Phenotype of gins1 mutant embryos and their siblings injected with 100 μM gins2MO. (F) Western blot analysis of protein lysates from 2 dpf control and gins1elu11/elu11 embryos probed with Gins1 and γ-tubulin antibodies. (G) Western blot analysis of protein lysates from wildtype embryos at the indicated stages probed with Gins1 and γ-tubulin antibodies. Scale bar: 250 μm.
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