Cold-sensitive growth and decreased GTP-hydrolytic activity from substitution of Pro17 for Val in Era, an essential Escherichia coli GTPase.

Abstract excerpt

A substitution mutation of Pro17 by Val (P17V) was constructed in the guanine nucleotide binding domain of Era, an essential protein in Escherichia coli. The mutation is analogous to the oncogenic activating allele at position 12 in the GTP-binding domain of p21ras. The phenotype of this mutant was analysed in a strain which exclusively expressed the mutant protein (Era-V17) in null allele chromosomal background...

Topics

• Bacterial Proteins
• Cold Temperature
• Escherichia coli
• Escherichia coli Proteins
• GTP Phosphohydrolases
• GTP-Binding Proteins
• Genes, Bacterial
• Mutagenesis, Site-Directed
• Phenotype
• Proline
• RNA-Binding Proteins