Mutations in the ATP-binding domain of Escherichia coli rho factor affect transcription termination in vivo.

Abstract excerpt

Five mutant rho proteins, representing alterations at three different locations in the Escherichia coli rho gene that affect ATP hydrolytic activity but not RNA binding, were examined in vivo for function at the rho-dependent IS2 and bacteriophage lambda tR1 terminators. The altered amino acids in rho are located at highly conserved residues near the beta 1 and beta 4 strands of the hydrophobic ATP-binding pocket...

Topics

• Adenosine Triphosphate
• Bacteriophage lambda
• Binding Sites
• Chromosome Mapping
• Escherichia coli
• Galactokinase
• Genes, Bacterial
• Mutation
• Plasmids
• Rho Factor
• Transcription Factors