Antignani, V., Klocko, A.L., Bak, G., Chandrasekaran, S.D., Dunivin, T., and Nielsen, E. (2015). Recruitment of PLANT U-BOX13 and the PI4Kβ1/β2 phosphatidylinositol-4 kinases by the small GTPase RabA4B plays important roles during salicylic acid-mediated plant defense signaling in Arabidopsis. Plant Cell 27: 243–261.
In Figure 1C, an image of a yeast two-hybrid drop assay was inadvertently duplicated (U-box domain interaction with GTP-bound RabA4b in –T and –LT growth conditions; circled in red in the original figure). In examining how this duplication occurred, we determined that images in the original figure also combined spots from two sets of replicate plates. Although these two sets of plates were spotted at the same time, used the same yeast strains, and presented virtually identical results, we now present images from only one set of plates in the corrected version of Figure 1C (all images replaced in this manner are underlined in red). In addition, we also now provide white borders between individual yeast spots in Figures 1A and 1C to indicate that they have been arranged in order to present this data in a more efficient and logical manner. Finally, “−HisTrpLeu” and “−HTL” were replaced with “−HisLeuTrp” and “−HLT,” respectively, in the figure legend to match the figure.
Figure 1.
Original: PUB13 Interacts Specifically with the Active Form of RabA4B.
(A) Y2H interaction of PUB13Δ552-660 with active GTP-bound RabA4B (T), but not inactive GDP-bound RabA4B (D), was detected on high-stringency medium (−HisTrpLeu + 3-aminotriazole [−HTL+3-AT]). No interaction was observed with RabF2A, RabG3C, and ROP1. The presence of prey and/or bait vectors was monitored by growth in the absence of leucine and tryptophan (−LT) or tryptophan (−T), respectively.
(B) UND, U-box, and ARM domains are indicated. Deletion fragments of PUB13 were constructed to determine the binding site of RabA4B.
(C) Y2H interaction was seen between active RabA4B and PUB13 fragments on selective medium (−HisTrpLeu+3-AT). The interaction between RabA4B and PUB13 requires the presence of UND and U-box domains. No interaction was observed between RabA4B and the ARM domain. Surprisingly, full-length PUB13 did not interact with RabA4B in the Y2H assay. (Inadvertently duplicated spots are circled in red).
Figure 1.
Corrected: PUB13 Interacts Specifically with the Active Form of RabA4B.
(A) Y2H interaction of PUB13Δ552-660 with active GTP-bound RabA4B (T), but not inactive GDP-bound RabA4B (D), was detected on high-stringency medium (−HisLeuTrp + 3-aminotriazole [−HLT+3-AT]). No interaction was observed with either form of RabF2A, RabG3C, and ROP1. The presence of prey and/or bait vectors was monitored by growth in the absence of leucine and tryptophan (−LT) or tryptophan (−T), respectively. Bait “T” and prey “p53” represent positive controls for interaction.
(B) UND, U-box, and ARM domains are indicated. Deletion fragments of PUB13 were constructed to determine the binding site of RabA4B.
(C) Y2H interaction was seen between active RabA4B (T) and PUB13 fragments on selective medium (−HLT+3-AT). The interaction between RabA4B and PUB13 requires the presence of UND and U-box domains. No interaction was observed between RabA4B and the ARM domain. Surprisingly, full-length PUB13 did not interact with RabA4B in the Y2H assay. Yeast spots grown in each selection condition were all from the same plate but rearranged in the figure for a logical order. Positive control as in (A). (Images that were replaced relative to the original figure are underlined in red).
Footnotes
Editor's note: the corrected figure and accompanying text were reviewed by members of The Plant Cell editorial board. Both the original and corrected figures are shown for ease of comparison.