Figure 3.
Figure 3. Localization of membrane-binding proteins in efr3Δ. (A) List of proteins tagged with GFP or mNG and screened for differences in protein localization in efr3Δ compared with WT. Fluorescence intensity at the division site was measured, and statistically significant differences are noted. (B–E, left) Live-cell imaging of Cdc15-GFP (B), Rgf1-GFP Sid4-GFP (C), Scd1-mNG (D), or Opy1-mNG (E) in either WT or efr3Δ. (B–D, middle) Quantification of fluorescence intensity at the cell division site. (E, middle) Line scan of fluorescence intensity. (B–E, right) Western blots of protein levels in WT and efr3Δ. Anti-PSTAIR was used to detect Cdc2, which served as a loading control. Measurements in B–D represent three biological replicates. Error bars represent SEM. **, P ≤ 0.01; ****, P ≤ 0.0001; Student’s t test. Bars, 2 µm. IB, immunoblot; IP, immunoprecipitation.

Localization of membrane-binding proteins in efr3Δ. (A) List of proteins tagged with GFP or mNG and screened for differences in protein localization in efr3Δ compared with WT. Fluorescence intensity at the division site was measured, and statistically significant differences are noted. (B–E, left) Live-cell imaging of Cdc15-GFP (B), Rgf1-GFP Sid4-GFP (C), Scd1-mNG (D), or Opy1-mNG (E) in either WT or efr3Δ. (B–D, middle) Quantification of fluorescence intensity at the cell division site. (E, middle) Line scan of fluorescence intensity. (B–E, right) Western blots of protein levels in WT and efr3Δ. Anti-PSTAIR was used to detect Cdc2, which served as a loading control. Measurements in B–D represent three biological replicates. Error bars represent SEM. **, P ≤ 0.01; ****, P ≤ 0.0001; Student’s t test. Bars, 2 µm. IB, immunoblot; IP, immunoprecipitation.

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