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

Mol Plant Microbe Interact. 1996 Sep;9(7):637-41. doi: 10.1094/mpmi-9-0637.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acids / metabolism
  • Bacterial Toxins / biosynthesis
  • Carrier Proteins / biosynthesis*
  • Carrier Proteins / isolation & purification
  • Cloning, Molecular / methods
  • Indenes / metabolism
  • Maltose
  • Maltose-Binding Proteins
  • Plasmids
  • Protein Biosynthesis*
  • Pseudomonas*
  • Recombinant Fusion Proteins / biosynthesis*
  • Recombinant Fusion Proteins / isolation & purification
  • Restriction Mapping

Substances

  • Amino Acids
  • Bacterial Toxins
  • Carrier Proteins
  • Indenes
  • Maltose-Binding Proteins
  • Recombinant Fusion Proteins
  • coronatine
  • Maltose