Article
The folding of the bifunctional TRP3 protein in yeast is influenced by a translational pause which lies in a region of structural divergence with Escherichia coli indoleglycerol-phosphate synthase.
European journal of biochemistry - 1 Dec 1994
Crombie T, Boyle J P, Coggins J R, Brown A J
Abstract excerpt
The yeast TRP3 gene encodes a bifunctional protein with anthranilate synthase II and indoleglycerol-phosphate synthase activities. Replacing ten consecutive non-preferred codons in the indoleglycerol-phosphate synthase region of the TRP3 gene with synonymous preferred codons (to create the TRP3pr...
Topics
- Amino Acid Sequence
- Anthranilate Synthase
- Escherichia coli
- HSP70 Heat-Shock Proteins
- Indole-3-Glycerol-Phosphate Synthase
- Models, Molecular
- Molecular Sequence Data
- Multienzyme Complexes
- Mutagenesis
- Mutation
- Protein Biosynthesis