USE OF TRANSLATIONAL FUSIONS TO THE MALTOSE-BINDING PROTEIN TO PRODUCE AND PURIFY PROTEINS IN PSEUDOMONAS-SYRINGAE AND ASSESS THEIR ACTIVITY IN-VIVO

A simple approach is described for the production and purification of proteins in Pseudomonas syringae. The strategy involves the use of the tac promoter,the maltose-binding protein, and the broad-host-range ve ctor, pRK415. This approach was used to partially purify two proteins involved in coronatine biosynthesis from P. syringae. The activity of the fusions was demonstrated in vivo in complementation experiments us ing the appropriate mutants.