Use of Translational Fusions to the Maltose-Binding Protein to Produce and Purify Proteins in Pseudomonas syringae and Assess Their Activity in Vivo. Alejandro Penaloza-Vazquez. (1)Department of Plant Pathology, Oklahoma State University, Stillwater, 74078-3032 U.S.A. and (2)Departamento de Ingenierfa Genetica de Plantas CINVESTAV-IPN Unidad Irapuato, Irapuato, Gto., 36500 Mexico. Vidhya Rangaswamy(1), Matthias Ullrich (1), Ana Maria Bailey (2),and Carol L. Bender(1). (1)Department of Plant Pathology, Oklahoma State University, Stillwater, 74078-3032 U.S.A. and (2)Departamento de Ingenierfa Genetica de Plantas CINVESTAV-IPN Unidad Irapuato, Irapuato, Gto., 36500 Mexico. MPMI 9:637-641. Accepted 15 May 1996. Copy right 1996 The American Phytopathological Society.

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 vector, 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 using the appropriate mutants.