The proximity of the C-terminal domain of Escherichia coli ribosomal protein L7/L12 to L10 determined by cysteine site-directed mutagenesis and protein-protein cross-linking.

Abstract excerpt

Oligonucleotide-directed mutagenesis was used to produce a serine 89 to cysteine 89 substitution in the C-terminal globular domain of Escherichia coli ribosomal protein L7/L12. Cys-89 represented the only cysteine residue in the protein. L7/L12Cys89 was overproduced in E. coli and purified. An allele replacement strain was also constructed. Growth of this strain was indistinguishable from that of wild type....

Topics

• Alleles
• Cross-Linking Reagents
• Cysteine
• Dithionitrobenzoic Acid
• Electrophoresis, Gel, Two-Dimensional
• Electrophoresis, Polyacrylamide Gel
• Escherichia coli
• Genetic Vectors
• Kinetics
• Macromolecular Substances