Truncated mutants of the colicin A lysis protein are acylated and processed when overproduced.
The lipid modification and processing of truncated mutants of the colicin A lysis protein were observed after overproduction by Escherichia coli bacteria, but at a rate far slower than that of the wild-type. The unmodified precursor form of the mutants was stable over hour(s). The truncated mutants provoked lethality, but neither caused protein release nor quasi-lysis.
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Centre de Biochimie et de Biologie Moléculaire, CNRS, Marseille, France.
D000215:Acylation; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism* / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects* / Q000235:genetics; D005990:Glycerol / Q000378:metabolism; D008074:Lipoproteins; D009154:Mutation; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000378:metabolism
D001426:Bacterial Proteins; C058485:CAL protein, Citrobacter freundii; D008074:Lipoproteins; D010169:Palmitic Acids; D011498:Protein Precursors; D011994:Recombinant Proteins; D019308:Palmitic Acid; D005990:Glycerol