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Use of Translational Fusions to the Maltose-Binding Protein to Produce and Purify Proteins inPseudomonas syringaeand Assess Their Activity in Vivo

Authors :
Matthias S. Ullrich
Rangaswamy
Alejandro Penaloza-Vazquez
Carol L. Bender
A M Bailey
Source :
Molecular Plant-Microbe Interactions. 9:637
Publication Year :
1996
Publisher :
Scientific Societies, 1996.

Abstract

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.

Details

ISSN :
08940282
Volume :
9
Database :
OpenAIRE
Journal :
Molecular Plant-Microbe Interactions
Accession number :
edsair.doi.dedup.....0ba94d43267331a936d200a0de2be229
Full Text :
https://doi.org/10.1094/mpmi-9-0637