PLANT BIOLOGY Correction for “SUMOylation of phytochrome-B negatively regulates light-induced signaling in Arabidopsis thaliana,” by Ari Sadanandom, Éva Ádám, Beatriz Orosa, András Viczián, Cornelia Klose, Cunjin Zhang, Eve-Marie Josse, László Kozma-Bognár, and Ferenc Nagy, which appeared in issue 35, September 1, 2015, of Proc Natl Acad Sci USA (112:11108–11113; first published August 17, 2015; 10.1073/pnas.1415260112).
The authors note that Fig. S2 and Fig. S8 appeared incorrectly. The SI has been corrected online.
Fig. S2.
(A) The abundance of phyB-GFP does not change significantly in seedlings grown under 12h L/12h D cycles. Transgenic phyB-9 seedlings expressing the 35S:PHYB-GFP transgene were grown in 12 h WL or RL/12 h D cycles for 5 d. Samples were harvested at MOD and MON of day 6. Total protein extracts were separated by SDS/PAGE. phyB-GFP and ACTIN proteins were detected using anti-GFP and anti-ACTIN antibodies, respectively. (B) Truncated phyB-YFP fusion proteins lacking Lys996 are not SUMOylated. Seedlings expressing full-length phyB (FL-phyB) and truncated phyB(1–651) or phyB(1–991) proteins fused to GFP or YFP were grown in darkness for 4 d (D) and transferred to WL for 24 h (W24). Fusion proteins were immunoprecipitated using GFP-Trap agarose beads (IP:αGFP). Samples containing comparable amounts of the different fusion proteins were separated by SDS/PAGE. Replicate Western blots were probed with anti-GFP (IB:αGFP) or anti-SUMO1 (IB:αSUMO1) antibodies. (C) Abundance of phyB-GFP and phyBLys996Arg-YFP fusion proteins expressed under the control of LIP1 and 35S promoters is identical pair-wise. Transgenic phyB-9 seedlings expressing the phyB-GFP fusion proteins were grown in darkness for 5 d. Total protein extracts were separated by SDS/PAGE. phyB-GFP and ACTIN proteins were detected using anti-GFP and anti-ACTIN antibodies, respectively. Results were obtained from independent phyBLys996Arg-YFP–expressing transgenic lines, 1 and 2 (Set 1 and Set 2). Separately framed images of the upper panels were produced from different blots.
Fig. S8.
OTS1 binds to phyB in planta. The Agrobacterium cultures containing the combination of constructs (phyB-GFP/HA-OTS1 or GFP/HA-OTS1) were infiltrated into N. benthamiana leaves. Three days after the Agrobacterium infiltration, the expression of the fusion proteins was confirmed by immunoblotting with anti-HA and anti-GFP antibodies (input panels). Coimmunoprecipitation assays performed with anti-GFP antibodies showed that HA-OTS1 immunoprecipitated with phyB-GFP but not with GFP alone, indicating that OTS1 interacts with phyB.