Killing of E coli cells by E group nuclease colicins.
The process by which the endonuclease domain of colicin E9 is translocated across the outer membrane, the periplasmic space and the cytoplasmic membrane to reach the cytoplasm of E. coli cells, resulting in DNA degradation and cell death, is a unique event in prokaryotic biology. Although considerable information is known about the role of the BtuB outer membrane receptor, as well as the mostly periplasmic Tol proteins that are essential for the translocation process, the precise nature of the interactions between colicin E9 and these proteins remains to be elucidated. In this review, we consider our current understanding of the key events in this process, concentrating on recent findings concerning receptor-binding, translocation and the mechanism of cytotoxicity.
James
Richard
R
Division of microbiology and infectious diseases, University Hospital, University of Nottingham, NG7 2UH, Nottingham, UK. richard.james@nottingham.ac.uk
Penfold
Christopher N
CN
Moore
Geoffrey R
GR
Kleanthous
Colin
C
D001425:Bacterial Outer Membrane Proteins; D002462:Cell Membrane / Q000378:metabolism; D003087:Colicins / Q000378:metabolism*; D003851:Deoxyribonucleases / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism; D026901:Membrane Transport Proteins; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D018000:Receptors, Peptide / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; C044592:BtuB protein, E coli; D003087:Colicins; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D018000:Receptors, Peptide; D003851:Deoxyribonucleases