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Updated: Jun 26, 2026

Quantitative Immunofluorescence to Measure Global Localized Translation
Published on: August 22, 2017
Maturation of the translation inhibitor microcin C
Anastasia Metlitskaya1, Teymur Kazakov, Gaston H Vondenhoff
1Institute of Molecular Genetics, Russian Academy of Sciences, Moscow, Russia.
Abstract:
Microcin C (McC), an inhibitor of the growth of enteric bacteria, consists of a heptapeptide with a modified AMP residue attached to the backbone of the C-terminal aspartate through an N-acyl phosphamidate bond. Here we identify maturation intermediates produced by cells lacking individual mcc McC biosynthesis genes. We show that the products of the mccD and mccE genes are required for attachment of a 3-aminopropyl group to the phosphate of McC and that this group increases the potency of inhibition of the McC target, aspartyl-tRNA synthetase.
Insights
Microcin C (McC) is a bacterial growth inhibitor. Its maturation involves specific gene products (mccD and mccE) that attach a 3-aminopropyl group, enhancing its potency against aspartyl-tRNA synthetase.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Microcin C (McC) is a heptapeptide antibiotic with a unique N-acyl phosphamidate bond linking a modified AMP residue.
- McC inhibits the growth of enteric bacteria by targeting aspartyl-tRNA synthetase.
Purpose of the Study:
- To identify maturation intermediates of Microcin C.
- To elucidate the roles of specific genes in the biosynthesis and maturation of Microcin C.
- To understand how post-translational modifications affect Microcin C's inhibitory activity.
Main Methods:
- Analysis of maturation intermediates in mutant strains lacking individual mcc biosynthesis genes.
- Biochemical characterization of Microcin C and its precursors.
Main Results:
- The products of the mccD and mccE genes are essential for the attachment of a 3-aminopropyl group to the phosphate of Microcin C.
- This 3-aminopropyl modification significantly increases the potency of Microcin C's inhibition of aspartyl-tRNA synthetase.
Conclusions:
- The maturation pathway of Microcin C involves specific enzymatic steps, including the addition of a 3-aminopropyl group.
- This modification is crucial for the enhanced biological activity of Microcin C against its target enzyme.
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