Format

Send to

Choose Destination
Mol Plant Microbe Interact. 1996 Sep;9(7):637-41.

Use of translational fusions to the maltose-binding protein to produce and purify proteins in Pseudomonas syringae and assess their activity in vivo.

Author information

1
Department of Plant Pathology, Oklahoma State University, Stillwater 74078-3032, USA.

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.

PMID:
8810079
DOI:
10.1094/mpmi-9-0637
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Atypon
Loading ...
Support Center