There were errors in J. Cell Sci. (2017) 130, jcs202853 ().
The wrong anti-His blots were used to prepare Fig. 5C and Fig. 7G. The corrected figure panels for tunicamycin-treated cells in Fig. 5C and TRX mutants in Fig. 7G are shown here. The anti-His blot for pH=8.5 cells in Fig. 5C was vertically compressed during figure preparation and therefore has also been updated. All analysis was carried out on the correct replicate blots and is not affected by these errors. The online and PDF versions of the article have been updated and the authors apologise to readers for the errors, which do not impact the conclusions of the paper.
Cch1p is glutathionylated under oxidative stress. (C) Glutathionylation of Cch1p in response to fast and slow activation. WT cells overexpressing Cch1p with OD600nm=1.5 were treated with 2 mM H2O2, pH 8.5, 1 µM tunicamycin or 0.5 µM α-factor for different time intervals. The blots were probed with mouse anti-His and mouse anti-GSH primary antibodies and goat anti-mouse-IgG conjugated to HRP as secondary antibody. Densitometry results (graphs) represent the mean±s.d. of three independent biological replicates. *P<0.05, **P<0.01, ***P<0.001.
Cch1p is glutathionylated under oxidative stress. (C) Glutathionylation of Cch1p in response to fast and slow activation. WT cells overexpressing Cch1p with OD600nm=1.5 were treated with 2 mM H2O2, pH 8.5, 1 µM tunicamycin or 0.5 µM α-factor for different time intervals. The blots were probed with mouse anti-His and mouse anti-GSH primary antibodies and goat anti-mouse-IgG conjugated to HRP as secondary antibody. Densitometry results (graphs) represent the mean±s.d. of three independent biological replicates. *P<0.05, **P<0.01, ***P<0.001.
Cch1p is glutathionylated under oxidative stress. (C) Glutathionylation of Cch1p in response to fast and slow activation. WT cells overexpressing Cch1p with OD600nm=1.5 were treated with 2 mM H2O2, pH 8.5, 1 μM tunicamycin or 0.5 μM α-factor for different time intervals. The blots were probed with mouse anti-His and mouse anti-GSH primary antibodies and goat anti-mouse-IgG conjugated to HRP as secondary antibody. Densitometry results (graphs) represent the mean±s.d. of three independent biological replicates. *P<0.05, **P<0.01, ***P<0.001.
Cch1p is glutathionylated under oxidative stress. (C) Glutathionylation of Cch1p in response to fast and slow activation. WT cells overexpressing Cch1p with OD600nm=1.5 were treated with 2 mM H2O2, pH 8.5, 1 μM tunicamycin or 0.5 μM α-factor for different time intervals. The blots were probed with mouse anti-His and mouse anti-GSH primary antibodies and goat anti-mouse-IgG conjugated to HRP as secondary antibody. Densitometry results (graphs) represent the mean±s.d. of three independent biological replicates. *P<0.05, **P<0.01, ***P<0.001.
Glutathionylation/deglutathionylation enzymes regulate Cch1 function. (G) Glutathionylation analysis of Yvc1p in TRX mutants.
