The Plant Cell, Volume 23, Issue 12, December 2011, Pages 4298–4317, https://doi.org/10.1105/tpc.111.089482
An inadvertent mistake in the assembly of Figure 6 of this manuscript resulted in a layer obscuring a portion of a blot shown in panel C. A corrected version of Figure 6 is shown below. The authors apologize for any inconvenience.
Figure 6.
rpt2a Mutants Destabilize the Arabidopsis 26S Proteasome. 26S proteasomes were enriched from 10-d-old liquid-grown seedlings of the indicated genotypes and subjected to glycerol gradient fractionation. (A) Total 26S proteasome activity in crude extracts. Equal amounts of crude extracts (based on total protein) were assayed for CP peptidase activity (6MG132) using the substrate Suc-LLVY-AMC. Each bar represents the average of triplicate assays (6SD). The asterisks indicate a significant difference between peptidase activity in the Col-0 wild type and mutants in the absence of MG132 (ANOVA followed by Tukey’s multiple comparisons post-test, P < 0.01). (B) Profile of CP peptidase activity across the glycerol gradient. Activity was measured in the absence or presence of 0.02% SDS using the substrate Suc-LLVY-AMC. The activity scale for each profile was adjusted to generate a near-equal height for the peak activity. The arrows delineate the range of fractions that were used for the immunoblot analyses in (C). (C) Immunoblot analyses of glycerol gradient fractions with antibodies prepared against various RP (RPT2, RPN1, RPN5, and RPN12a) and CP (PAG1 and PBA1) subunits of the 26S proteasome. The locations of the 26S proteasome and the CP and RP subcomplexes, as determined by peptidase activity and immunoblot analysis, are indicated by the brackets.
Editors’ note: This correction notice was reviewed by members of The Plant Cell editorial board. The authors are responsible for providing a complete listing and accurate explanations for all known errors or instances of inappropriate data handling or image manipulation associated with the original publication.