Abstract
The heptapeptide-nucleotide microcin C (McC) targets aspartyl-tRNA synthetase. Upon its entry into a susceptible cell, McC is processed to release a nonhydrolyzable aspartyl-adenylate that inhibits aspartyl-tRNA synthetase, leading to the cessation of translation and cell growth. Here, we surveyed Escherichia coli cells with singly, doubly, and triply disrupted broad-specificity peptidase genes to show that any of three nonspecific oligopeptidases (PepA, PepB, or PepN) can effectively process McC. We also show that the rate-limiting step of McC processing in vitro is deformylation of the first methionine residue of McC.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Monophosphate / analogs & derivatives
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Adenosine Monophosphate / metabolism
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Adenosine Monophosphate / pharmacology
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Aminopeptidases / genetics
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Aminopeptidases / metabolism
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Aspartate-tRNA Ligase / antagonists & inhibitors
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Aspartate-tRNA Ligase / metabolism
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Aspartic Acid / analogs & derivatives
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Aspartic Acid / metabolism
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Aspartic Acid / pharmacology
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Bacteriocins / chemistry
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Bacteriocins / metabolism*
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Mass Spectrometry
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Metalloendopeptidases / genetics
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Metalloendopeptidases / metabolism
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Molecular Structure
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Mutation
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Peptide Hydrolases / genetics
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Peptide Hydrolases / metabolism*
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Serine Endopeptidases / genetics
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Serine Endopeptidases / metabolism
Substances
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Bacterial Proteins
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Bacteriocins
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Escherichia coli Proteins
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pepN protein, Bacteria
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aspartyl adenylate
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Aspartic Acid
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Adenosine Monophosphate
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Peptide Hydrolases
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oligopeptidase
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Aminopeptidases
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Serine Endopeptidases
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oligopeptidase B
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Metalloendopeptidases
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oligopeptidase A
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Aspartate-tRNA Ligase