Skip to main content
. 2005 Jan;187(2):649–663. doi: 10.1128/JB.187.2.649-663.2005

FIG. 3.

FIG. 3.

HopB1 and HrpK are translocated into plant cells based on reporter assays; however, HrpK requires its C-terminal half to translocate. (A) AvrRpt2 translocation assays with HopB1 and HrpK AvrRpt2 fusions. P. syringae pv. phaseolicola NPS3121 carrying constructs that encoded either full-length AvrRpt2, an 80-amino-acid N-terminal deletion of AvrRpt2 (ΔAvrRpt2), full-length HopB1 fused to ΔAvrRpt2 (HopB1-ΔAvrRpt2), full-length HrpK fused to ΔAvrRpt2 (HrpK-ΔAvrRpt2), and the first 399 amino acids of HrpK fused to ΔAvrRpt2 (HrpK1-399-ΔAvrRpt2) were infiltrated into A. thaliana Col-0 at an OD600 of 0.5 and scored after 12 to 19 h for elicitation of the HR. N, no visible HR. (B) CyaA translocation assays with HopB1 and HrpK CyaA fusions. DC3000 and a DC3000 hrcC mutant defective in TTSS carrying constructs that encoded either full-length HopB1 (HopB1-CyaA), HrpK (HrpK-CyaA), or the first 382 amino acids of HrpK (HrpK1-382-CyaA) fused to CyaA were infiltrated into N. benthamiana and assayed for cAMP production 7 h after infiltration as described in Materials and Methods. cAMP levels are reported in picomoles of cAMP per micrograms of protein with standard errors. The levels of cAMP indicated that the full-length HopB1-CyaA fusion and the full-length HrpK-CyaA fusion were translocated. However, the N-terminal HrpK-CyaA fusion had background levels of cAMP, indicating that it was not translocated.