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(A) DND1 (purple) and NANOS3 (pink) residues interacting with the N3-DRE. Filled shading, residues substituted with alanine for functional analysis. (B) DND1–NANOS3 co-expression constructs with indicated mutations (top) or truncations (bottom). (C) Schematic of assays performed with cells expressing constructs from (B). (D) Assay results for DND1–NANOS3 constructs with DND1 point mutants: ( 1 ) IncuCyte growth assays; ( 2 ) expression of N3-DRE-containing <t>RNAs;</t> ( 3 ) protein levels of N3-DRE-containing targets (CDK1, EHMT2, and CNOT6; immunoblots in Fig. S5 ). (E) As in (D), with NANOS3 point mutations. (F) DND1 K196A loses selectivity for the N3-DRE G3 nucleotide in vitro . Error bars, K d confidence interval from MST data fitting. (G) As in (D), with DND1 or NANOS3 truncations. (H) Effects of DND1/NANOS3 mutations or deletions on RNA turnover. Left, median fold changes in k deg for each N3-DRE class, normalized to the corresponding No motif group. Middle, median fold changes in k syn . Right, median fold changes in transcript half-life. Corresponding violin plots and CDFs are shown in Figures S5F and S5G . (I) Summary of the functional impact of RNA-binding residue mutations and IDR deletion. Statistics (D-F): Cell growth: Scale bar, 400 μm (bottom right image only). CDFs: n, number of genes; ML, median log 2 -fold change; δ, Cliff’s delta; p , two-sided Wilcoxon rank-sum test. Protein quantification: Error bars indicate S.D. Two-sided Student’s t -test ( n = 3 independent experiments). Exact p -values are provided in Source Data. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. See also Figure S5 and Table S1 .
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(A) DND1 (purple) and NANOS3 (pink) residues interacting with the N3-DRE. Filled shading, residues substituted with alanine for functional analysis. (B) DND1–NANOS3 co-expression constructs with indicated mutations (top) or truncations (bottom). (C) Schematic of assays performed with cells expressing constructs from (B). (D) Assay results for DND1–NANOS3 constructs with DND1 point mutants: ( 1 ) IncuCyte growth assays; ( 2 ) expression of N3-DRE-containing <t>RNAs;</t> ( 3 ) protein levels of N3-DRE-containing targets (CDK1, EHMT2, and CNOT6; immunoblots in Fig. S5 ). (E) As in (D), with NANOS3 point mutations. (F) DND1 K196A loses selectivity for the N3-DRE G3 nucleotide in vitro . Error bars, K d confidence interval from MST data fitting. (G) As in (D), with DND1 or NANOS3 truncations. (H) Effects of DND1/NANOS3 mutations or deletions on RNA turnover. Left, median fold changes in k deg for each N3-DRE class, normalized to the corresponding No motif group. Middle, median fold changes in k syn . Right, median fold changes in transcript half-life. Corresponding violin plots and CDFs are shown in Figures S5F and S5G . (I) Summary of the functional impact of RNA-binding residue mutations and IDR deletion. Statistics (D-F): Cell growth: Scale bar, 400 μm (bottom right image only). CDFs: n, number of genes; ML, median log 2 -fold change; δ, Cliff’s delta; p , two-sided Wilcoxon rank-sum test. Protein quantification: Error bars indicate S.D. Two-sided Student’s t -test ( n = 3 independent experiments). Exact p -values are provided in Source Data. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. See also Figure S5 and Table S1 .
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(A) DND1 (purple) and NANOS3 (pink) residues interacting with the N3-DRE. Filled shading, residues substituted with alanine for functional analysis. (B) DND1–NANOS3 co-expression constructs with indicated mutations (top) or truncations (bottom). (C) Schematic of assays performed with cells expressing constructs from (B). (D) Assay results for DND1–NANOS3 constructs with DND1 point mutants: ( 1 ) IncuCyte growth assays; ( 2 ) expression of N3-DRE-containing <t>RNAs;</t> ( 3 ) protein levels of N3-DRE-containing targets (CDK1, EHMT2, and CNOT6; immunoblots in Fig. S5 ). (E) As in (D), with NANOS3 point mutations. (F) DND1 K196A loses selectivity for the N3-DRE G3 nucleotide in vitro . Error bars, K d confidence interval from MST data fitting. (G) As in (D), with DND1 or NANOS3 truncations. (H) Effects of DND1/NANOS3 mutations or deletions on RNA turnover. Left, median fold changes in k deg for each N3-DRE class, normalized to the corresponding No motif group. Middle, median fold changes in k syn . Right, median fold changes in transcript half-life. Corresponding violin plots and CDFs are shown in Figures S5F and S5G . (I) Summary of the functional impact of RNA-binding residue mutations and IDR deletion. Statistics (D-F): Cell growth: Scale bar, 400 μm (bottom right image only). CDFs: n, number of genes; ML, median log 2 -fold change; δ, Cliff’s delta; p , two-sided Wilcoxon rank-sum test. Protein quantification: Error bars indicate S.D. Two-sided Student’s t -test ( n = 3 independent experiments). Exact p -values are provided in Source Data. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. See also Figure S5 and Table S1 .
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(A) DND1 (purple) and NANOS3 (pink) residues interacting with the N3-DRE. Filled shading, residues substituted with alanine for functional analysis. (B) DND1–NANOS3 co-expression constructs with indicated mutations (top) or truncations (bottom). (C) Schematic of assays performed with cells expressing constructs from (B). (D) Assay results for DND1–NANOS3 constructs with DND1 point mutants: ( 1 ) IncuCyte growth assays; ( 2 ) expression of N3-DRE-containing <t>RNAs;</t> ( 3 ) protein levels of N3-DRE-containing targets (CDK1, EHMT2, and CNOT6; immunoblots in Fig. S5 ). (E) As in (D), with NANOS3 point mutations. (F) DND1 K196A loses selectivity for the N3-DRE G3 nucleotide in vitro . Error bars, K d confidence interval from MST data fitting. (G) As in (D), with DND1 or NANOS3 truncations. (H) Effects of DND1/NANOS3 mutations or deletions on RNA turnover. Left, median fold changes in k deg for each N3-DRE class, normalized to the corresponding No motif group. Middle, median fold changes in k syn . Right, median fold changes in transcript half-life. Corresponding violin plots and CDFs are shown in Figures S5F and S5G . (I) Summary of the functional impact of RNA-binding residue mutations and IDR deletion. Statistics (D-F): Cell growth: Scale bar, 400 μm (bottom right image only). CDFs: n, number of genes; ML, median log 2 -fold change; δ, Cliff’s delta; p , two-sided Wilcoxon rank-sum test. Protein quantification: Error bars indicate S.D. Two-sided Student’s t -test ( n = 3 independent experiments). Exact p -values are provided in Source Data. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. See also Figure S5 and Table S1 .
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(A) DND1 (purple) and NANOS3 (pink) residues interacting with the N3-DRE. Filled shading, residues substituted with alanine for functional analysis. (B) DND1–NANOS3 co-expression constructs with indicated mutations (top) or truncations (bottom). (C) Schematic of assays performed with cells expressing constructs from (B). (D) Assay results for DND1–NANOS3 constructs with DND1 point mutants: ( 1 ) IncuCyte growth assays; ( 2 ) expression of N3-DRE-containing <t>RNAs;</t> ( 3 ) protein levels of N3-DRE-containing targets (CDK1, EHMT2, and CNOT6; immunoblots in Fig. S5 ). (E) As in (D), with NANOS3 point mutations. (F) DND1 K196A loses selectivity for the N3-DRE G3 nucleotide in vitro . Error bars, K d confidence interval from MST data fitting. (G) As in (D), with DND1 or NANOS3 truncations. (H) Effects of DND1/NANOS3 mutations or deletions on RNA turnover. Left, median fold changes in k deg for each N3-DRE class, normalized to the corresponding No motif group. Middle, median fold changes in k syn . Right, median fold changes in transcript half-life. Corresponding violin plots and CDFs are shown in Figures S5F and S5G . (I) Summary of the functional impact of RNA-binding residue mutations and IDR deletion. Statistics (D-F): Cell growth: Scale bar, 400 μm (bottom right image only). CDFs: n, number of genes; ML, median log 2 -fold change; δ, Cliff’s delta; p , two-sided Wilcoxon rank-sum test. Protein quantification: Error bars indicate S.D. Two-sided Student’s t -test ( n = 3 independent experiments). Exact p -values are provided in Source Data. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. See also Figure S5 and Table S1 .
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(A) DND1 (purple) and NANOS3 (pink) residues interacting with the N3-DRE. Filled shading, residues substituted with alanine for functional analysis. (B) DND1–NANOS3 co-expression constructs with indicated mutations (top) or truncations (bottom). (C) Schematic of assays performed with cells expressing constructs from (B). (D) Assay results for DND1–NANOS3 constructs with DND1 point mutants: ( 1 ) IncuCyte growth assays; ( 2 ) expression of N3-DRE-containing <t>RNAs;</t> ( 3 ) protein levels of N3-DRE-containing targets (CDK1, EHMT2, and CNOT6; immunoblots in Fig. S5 ). (E) As in (D), with NANOS3 point mutations. (F) DND1 K196A loses selectivity for the N3-DRE G3 nucleotide in vitro . Error bars, K d confidence interval from MST data fitting. (G) As in (D), with DND1 or NANOS3 truncations. (H) Effects of DND1/NANOS3 mutations or deletions on RNA turnover. Left, median fold changes in k deg for each N3-DRE class, normalized to the corresponding No motif group. Middle, median fold changes in k syn . Right, median fold changes in transcript half-life. Corresponding violin plots and CDFs are shown in Figures S5F and S5G . (I) Summary of the functional impact of RNA-binding residue mutations and IDR deletion. Statistics (D-F): Cell growth: Scale bar, 400 μm (bottom right image only). CDFs: n, number of genes; ML, median log 2 -fold change; δ, Cliff’s delta; p , two-sided Wilcoxon rank-sum test. Protein quantification: Error bars indicate S.D. Two-sided Student’s t -test ( n = 3 independent experiments). Exact p -values are provided in Source Data. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. See also Figure S5 and Table S1 .
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(A) DND1 (purple) and NANOS3 (pink) residues interacting with the N3-DRE. Filled shading, residues substituted with alanine for functional analysis. (B) DND1–NANOS3 co-expression constructs with indicated mutations (top) or truncations (bottom). (C) Schematic of assays performed with cells expressing constructs from (B). (D) Assay results for DND1–NANOS3 constructs with DND1 point mutants: ( 1 ) IncuCyte growth assays; ( 2 ) expression of N3-DRE-containing <t>RNAs;</t> ( 3 ) protein levels of N3-DRE-containing targets (CDK1, EHMT2, and CNOT6; immunoblots in Fig. S5 ). (E) As in (D), with NANOS3 point mutations. (F) DND1 K196A loses selectivity for the N3-DRE G3 nucleotide in vitro . Error bars, K d confidence interval from MST data fitting. (G) As in (D), with DND1 or NANOS3 truncations. (H) Effects of DND1/NANOS3 mutations or deletions on RNA turnover. Left, median fold changes in k deg for each N3-DRE class, normalized to the corresponding No motif group. Middle, median fold changes in k syn . Right, median fold changes in transcript half-life. Corresponding violin plots and CDFs are shown in Figures S5F and S5G . (I) Summary of the functional impact of RNA-binding residue mutations and IDR deletion. Statistics (D-F): Cell growth: Scale bar, 400 μm (bottom right image only). CDFs: n, number of genes; ML, median log 2 -fold change; δ, Cliff’s delta; p , two-sided Wilcoxon rank-sum test. Protein quantification: Error bars indicate S.D. Two-sided Student’s t -test ( n = 3 independent experiments). Exact p -values are provided in Source Data. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. See also Figure S5 and Table S1 .
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(A) DND1 (purple) and NANOS3 (pink) residues interacting with the N3-DRE. Filled shading, residues substituted with alanine for functional analysis. (B) DND1–NANOS3 co-expression constructs with indicated mutations (top) or truncations (bottom). (C) Schematic of assays performed with cells expressing constructs from (B). (D) Assay results for DND1–NANOS3 constructs with DND1 point mutants: ( 1 ) IncuCyte growth assays; ( 2 ) expression of N3-DRE-containing <t>RNAs;</t> ( 3 ) protein levels of N3-DRE-containing targets (CDK1, EHMT2, and CNOT6; immunoblots in Fig. S5 ). (E) As in (D), with NANOS3 point mutations. (F) DND1 K196A loses selectivity for the N3-DRE G3 nucleotide in vitro . Error bars, K d confidence interval from MST data fitting. (G) As in (D), with DND1 or NANOS3 truncations. (H) Effects of DND1/NANOS3 mutations or deletions on RNA turnover. Left, median fold changes in k deg for each N3-DRE class, normalized to the corresponding No motif group. Middle, median fold changes in k syn . Right, median fold changes in transcript half-life. Corresponding violin plots and CDFs are shown in Figures S5F and S5G . (I) Summary of the functional impact of RNA-binding residue mutations and IDR deletion. Statistics (D-F): Cell growth: Scale bar, 400 μm (bottom right image only). CDFs: n, number of genes; ML, median log 2 -fold change; δ, Cliff’s delta; p , two-sided Wilcoxon rank-sum test. Protein quantification: Error bars indicate S.D. Two-sided Student’s t -test ( n = 3 independent experiments). Exact p -values are provided in Source Data. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. See also Figure S5 and Table S1 .
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Image Search Results


(A) DND1 (purple) and NANOS3 (pink) residues interacting with the N3-DRE. Filled shading, residues substituted with alanine for functional analysis. (B) DND1–NANOS3 co-expression constructs with indicated mutations (top) or truncations (bottom). (C) Schematic of assays performed with cells expressing constructs from (B). (D) Assay results for DND1–NANOS3 constructs with DND1 point mutants: ( 1 ) IncuCyte growth assays; ( 2 ) expression of N3-DRE-containing RNAs; ( 3 ) protein levels of N3-DRE-containing targets (CDK1, EHMT2, and CNOT6; immunoblots in Fig. S5 ). (E) As in (D), with NANOS3 point mutations. (F) DND1 K196A loses selectivity for the N3-DRE G3 nucleotide in vitro . Error bars, K d confidence interval from MST data fitting. (G) As in (D), with DND1 or NANOS3 truncations. (H) Effects of DND1/NANOS3 mutations or deletions on RNA turnover. Left, median fold changes in k deg for each N3-DRE class, normalized to the corresponding No motif group. Middle, median fold changes in k syn . Right, median fold changes in transcript half-life. Corresponding violin plots and CDFs are shown in Figures S5F and S5G . (I) Summary of the functional impact of RNA-binding residue mutations and IDR deletion. Statistics (D-F): Cell growth: Scale bar, 400 μm (bottom right image only). CDFs: n, number of genes; ML, median log 2 -fold change; δ, Cliff’s delta; p , two-sided Wilcoxon rank-sum test. Protein quantification: Error bars indicate S.D. Two-sided Student’s t -test ( n = 3 independent experiments). Exact p -values are provided in Source Data. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. See also Figure S5 and Table S1 .

Journal: Molecular cell

Article Title: DND1–NANOS3 shapes the PGC transcriptome via a heptanucleotide sequence in mRNA 3′-UTRs

doi: 10.1016/j.molcel.2026.09.010

Figure Lengend Snippet: (A) DND1 (purple) and NANOS3 (pink) residues interacting with the N3-DRE. Filled shading, residues substituted with alanine for functional analysis. (B) DND1–NANOS3 co-expression constructs with indicated mutations (top) or truncations (bottom). (C) Schematic of assays performed with cells expressing constructs from (B). (D) Assay results for DND1–NANOS3 constructs with DND1 point mutants: ( 1 ) IncuCyte growth assays; ( 2 ) expression of N3-DRE-containing RNAs; ( 3 ) protein levels of N3-DRE-containing targets (CDK1, EHMT2, and CNOT6; immunoblots in Fig. S5 ). (E) As in (D), with NANOS3 point mutations. (F) DND1 K196A loses selectivity for the N3-DRE G3 nucleotide in vitro . Error bars, K d confidence interval from MST data fitting. (G) As in (D), with DND1 or NANOS3 truncations. (H) Effects of DND1/NANOS3 mutations or deletions on RNA turnover. Left, median fold changes in k deg for each N3-DRE class, normalized to the corresponding No motif group. Middle, median fold changes in k syn . Right, median fold changes in transcript half-life. Corresponding violin plots and CDFs are shown in Figures S5F and S5G . (I) Summary of the functional impact of RNA-binding residue mutations and IDR deletion. Statistics (D-F): Cell growth: Scale bar, 400 μm (bottom right image only). CDFs: n, number of genes; ML, median log 2 -fold change; δ, Cliff’s delta; p , two-sided Wilcoxon rank-sum test. Protein quantification: Error bars indicate S.D. Two-sided Student’s t -test ( n = 3 independent experiments). Exact p -values are provided in Source Data. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. See also Figure S5 and Table S1 .

Article Snippet: We purchased a cocktail of three small guide RNAs (sgRNAs) (Santa Cruz Biotechnology, Inc., sc-434074), cloned individual sgRNA plasmids, and used pairs of the sgRNAs for the targeted deletions of the ZF region of the Nanos3 locus.

Techniques: RNA Binding Assay, Functional Assay, Analysis, Expressing, Construct, Western Blot, In Vitro, Residue