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Correction for Day et al., Plant Cell 18 (10) 2782-2791.
First published online August 24, 2007; 10.1105/tpc.107.190861

The Plant Cell 19:2691-2692 (2007)
© 2007 American Society of Plant Biologists

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Correction

Brad Day, Douglas Dahlbeck, and Brian J. Staskawicz (2006). NDR1 Interaction with RIN4 Mediates the Differential Activation of Multiple Disease Resistance Pathways in Arabidopsis. Plant Cell 18: 2782–2791.

In Figure 5A , sections of a protein gel image were inadvertently inserted that also had appeared in Figure 6. In addition, a single leaf panel was duplicated in Figure 7C . The experiments have been repeated as independent confirmation of the data, and the corrected images for Figures 5A and 7C appear below. Please note that all references to Figure 7 in the Results, Methods, and Discussion with regard to (previous) AvrB should now be replaced with AvrRpm1.


Figure 1
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  		Figure 5. The NDR1–RIN4 Interaction Occurs within the First Four Amino Acids of NDR1.

Stepwise deletions of two and four amino acids from the N terminus of NDR1 results in a differential pattern of association with RIN4.

(A) Coimmunoprecipitation and protein gel blot analysis of T7:NDR1 and HA:RIN4 from total protein extracts isolated from transiently expressed N. benthamiana. Loss of the NDR1–RIN4 interaction occurs following deletion of four amino acids from the N terminus of NDR1.

(B) Homologous expression of the NDR1{Delta}4 deletion mutant in Arabidopsis. Native promoter expression of T7:NDR1 and T7:NDR1{Delta}4 cDNAs in the Arabidopsis ndr1-1 mutant background confirms results of transient heterologous expression. Native RIN4 antibodies coimmunoprecipitate T7:NDR1 yet fail to coimmunoprecipitate T7:NDR1{Delta}4.

(C) Ultracentrifugation and localization of NDR1 and NDR1 deletion constructs confirm membrane localization. Total protein extracts from Arabidopsis plants (ndr1-1/HA:NDR1) expressing wild-type and deletion constructs were subjected to ultracentrifugation and separation by SDS-PAGE. Protein gel blot analysis (anti-T7) confirms plasma membrane localization for wild-type, {Delta}2, and {Delta}4 T7:NDR1 constructs.

 

Figure 2
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  		Figure 7. Construction of a Homologous Expression System for Characterizing the RPS2–RIN4–NDR1 Interaction.

(A) rps2/ndr1-1 mutant Arabidopsis plants were transformed with a dual promoter construct expressing RPS2:HA and T7:NDR1/T7:NDR1{Delta}4 expressed under the control of their respective native promoters.

(B) Protein gel blot analysis of RPS2:HA/T7:NDR1 and RPS2:HA/T7:NDR1{Delta}4 transgenic plants. Total protein extracts were separated by SDS-PAGE and probed with anti-HA antibodies (RPS2) and anti-T7 (NDR1) to determine protein expression levels in complemented Arabidopsis lines.

(C) High-density (5 x 107 colony-forming units [cfu]/mL) inoculation of wild-type Col-0 (top panels), RPS2:HA/T7:NDR1 (middle panels), and RPS2:HA/T7:NDR1{Delta}4 (bottom panels) with P. syringae DC3000 expressing empty vector (EV; control), AvrRpt2, AvrRpm1, and AvrPphB effector proteins.

(D) Bacterial growth curve analysis of native promoter expression lines of Arabidopsis RPS2:HA/T7:NDR1- and RPS2:HA/T7:NDR1{Delta}4-complemented plants. Bacterial counts were determined at days 0 and 4 following inoculation with P. syringae strains (104 cfu/mL) expressing the indicated effector protein. Day 0 controls were plated 1 h after inoculation and represent the average bacterial growth count of all plant genotypes tested. The Arabidopsis ndr1-1/rps2 genotype corresponds to the parent genotype of the complemented expression system shown in (A). Data shown are the mean of four independent lines for both RPS2:HA/T7:NDR1 and RPS2:HA/T7:NDR1{Delta}4 constructs. Error bars indicate standard deviation calculated from the mean of replicate samples.

 
Footnotes

www.plantcell.org/cgi/doi/10.1105/tpc.107.190861





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