CORRECTION

Choudhury, S.R., Pandey, S. (2015). Phosphorylation-dependent regulation of G-protein cycle during nodule formation in soybean. Plant Cell 27: 3260–3276; DOI: https://doi.org/10.1105/tpc.15.00517.

In Figure 7B and Supplemental Figure 10, showing BiFC-based interaction between NFR1 and RGS proteins, some of the images were inadvertently duplicated (i.e., the same representative image was used for showing different interaction combinations). In addition, images from experiments performed at different time points were assembled in one panel, which had affected the contrast and brightness in certain cases. To address these discrepancies, we have included all images taken in a single experiment in the assembled panels for both the figures. The corrected figures are presented below.

Figure 7.

Soybean RGS Proteins Interact with NFR1 Receptors.

(B) Interaction between RGS (in 77-nEYFP-N1) and NFR1 (in 78-cEYFP-N1) proteins using BiFC assay. Agrobacteria containing different combinations of RGS1 and RGS2 and NFR1α were infiltrated in tobacco leaves, and reconstitution of YFP fluorescence due to protein-protein interaction was visualized using a Nikon Eclipse E800 microscope with epifluorescence modules. At least four independent infiltrations were performed for each protein combination with similar results.

In Supplemental Figure 16B, showing split ubiquitin-based interaction between NFR1α and RGS2 C-ter, the image was not labeled. The labeled figure is presented below.

Supplemental Figure 10.

Interaction between RGS (in 77-nEYFP-N1) and NFR1 (in 78-cEYFP-N1) proteins using bimolecular fluorescence complementation assay.

Agrobacteria containing different combination of soybean RGS1 and RGS2 and NFR1 (α, β) proteins were infiltrated in tobacco leaves, and reconstitution of YFP fluorescence due to protein-protein interaction was recorded. Infiltrated plants were incubated in darkness for 24 h followed by 36 h incubation in light. The leaves were observed under Nikon Eclipse E800 microscope with epifluorescent modules for YFP fluorescence detection. At least five independent infiltrations were performed for each construct. (A) Interaction between full-length and N- and C-terminal RGS proteins with NFR1β protein using bimolecular fluorescence complementation assay. (B) The interaction combinations are: RGS1/RGS2 + NFR1α N-terminal, RGS1/RGS2 + NFR1β N-terminal, RGS1/RGS2 + NFR1α C-terminal, RGS1/RGS2 + NFR1β C-terminal, RGS1/RGS2 + EV. Interactions between soybean RGS1 and RGS2 with empty vector were used as negative controls.

Supplemental Figure 16.

Interaction between Gα proteins with wild type and mutant RGS2 and NFR1α proteins using split-ubiquitin-based interaction assay.

(B) C-terminal RGS protein was used as CUb fusion (RGS-CUb) and NFR1α proteins were used as NUb fusions in both orientations. The interaction combinations are: (1) C-terminal RGS2-CUb + NFR1α-NUb; (2) C-terminal RGS2^S405A-CUb + NFR1α-NUb; (3) C-terminal RGS2^HexaA-CUb + NFR1α-NUb; (4) C-terminal RGS2-CUb + NUb-NFR1α; (5) C-terminal RGS2^S405A-CUb + NUb-NFR1α; (6) C-terminal RGS2^HexaA-CUb + NUb-NFR1α; (7) C-terminal RGS2-CUb + NUbwt-NFR1α (positive control); and (8) C-terminal RGS2-Cub + NUb-vector (negative control).

These corrections do not affect the figure legends, results, or any of the conclusions. We apologize for any inconvenience this may have caused to the readers. Both authors agree to these corrections.

Editors’ note: The corrected figures and accompanying text were 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.