Thermodynamic consequences of bipartite immunity protein binding to the ribosomal ribonuclease colicin E3.

Journal article

Colicin E3 is a 60 kDa, multidomain protein antibiotic that targets its ribonuclease activity to an essential region of the 16S ribosomal RNA of Escherichia coli. To prevent suicide of the producing cell, synthesis of the toxin is accompanied by the production of a 10 kDa immunity protein (Im3) that binds strongly to the toxin and abolishes its enzymatic activity. In the present work, we study the interaction of Im3 with the isolated cytotoxic domain (E3 rRNase) and intact colicin E3 through ...

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Authors: Walker, D; Moore, G; James, R; Kleanthous, K

• Journal: Biochemistry
• Volume: 42
• Issue: 14
• Pages: 4161-4171
• Publication date: 2003-04-01
• DOI: 10.1021/bi0273720
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Plasmids; Kinetics; Protein Binding; Protein Folding; Thermodynamics; Bacterial Proteins; Colicins; Calorimetry; Spectrometry, Fluorescence