Article
Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemi.
Molecular microbiology - 1 Feb 1994
Bortoli-German I, Brun E, Py B, Chippaux M, Barras F
Abstract excerpt
Secretion to the cell exterior of cellulase EGZ and of at least six pectinases enables the Gram-negative Erwinia chrysanthemi to cause severe plant disease. The C-terminal cellulose-binding domain (CBD) of EGZ was found to contain a disulphide bond which forms, in the periplasm, between residues Cys-325 and Cys-382. Dithiothreitol (DTT)-treatment of native EGZ showed that the disulphide bond was dispensable, both...
Topics
- Amino Acid Sequence
- Base Sequence
- Cellulase
- Cellulose
- Dickeya chrysanthemi
- Disulfides
- Dithiothreitol
- Enzyme Stability
- Escherichia coli
- Molecular Sequence Data
- Mutation