PMID:11511369
| Citation |
de Zamaroczy, M, Mora, L, Lecuyer, A, Géli, V and Buckingham, RH (2001) Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase LepB. Mol. Cell 8:159-68 |
|---|---|
| Abstract |
Colicin D is known to kill target cells by cleaving tRNA(Arg). A colicin D-resistant mutant was selected that was altered in the inner membrane leader peptidase, LepB. The substituted residue (Asn274Lys) is located close to the catalytic site. The mutation abolishes colicin D cleavage but not the processing of exported proteins. LepB is required for colicin D cleavage, releasing a small C-terminal fragment that retains full tRNase activity. The immunity protein was found to prevent colicin D processing and furthermore masks tRNase activity, thus protecting colicin D against LepB-mediated cleavage during export. Catalytic colicins share a consensus sequence at their putative processing site. Mutations affecting normal processing of colicin D abolish cytotoxicity without affecting the in vitro tRNase activity. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Blotting, Northern; Catalytic Domain; Colicins/chemistry; Colicins/genetics; Colicins/metabolism; Colicins/pharmacology; Escherichia coli/physiology; Genetic Complementation Test; Membrane Proteins; Models, Molecular; Molecular Sequence Data; Point Mutation; Protein Structure, Tertiary; Pyocins/metabolism; RNA, Transfer/metabolism; Ribonucleases/chemistry; Ribonucleases/genetics; Ribonucleases/metabolism; Sequence Alignment; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism; Temperature |
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