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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
- 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.
- Subjects :
- Physiology
Recombinant Fusion Proteins
Bacterial Toxins
Restriction Mapping
Mutant
Maltose-Binding Proteins
law.invention
Maltose-binding protein
chemistry.chemical_compound
law
Pseudomonas
Pseudomonas syringae
Amino Acids
Cloning, Molecular
Maltose
biology
Coronatine
General Medicine
biology.organism_classification
Complementation
Indenes
chemistry
Biochemistry
Protein Biosynthesis
Pseudomonadales
biology.protein
Recombinant DNA
Carrier Proteins
Agronomy and Crop Science
Plasmids
Pseudomonadaceae
Subjects
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