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Published on: April 26, 2019
Low-molecular-weight post-translationally modified microcins
Konstantin Severinov1, Ekaterina Semenova, Alexey Kazakov
1Waksman Institute for Microbiology, Rutgers, the State University of New Jersey, Piscataway, NJ 08854, USA. severik@waksman.rutgers.edu
Abstract:
Microcins are a class of ribosomally synthesized antibacterial peptides produced by Enterobacteriaceae and active against closely related bacterial species. While some microcins are active as unmodified peptides, others are heavily modified by dedicated maturation enzymes. Low-molecular-weight microcins from the post-translationally modified group target essential molecular machines inside the cells. In this review, available structural and functional data about three such microcins--microcin J25, microcin B17 and microcin C7-C51--are discussed. While all three low-molecular-weight post-translationally modified microcins are produced by Escherichia coli, inferences based on sequence and structural similarities with peptides encoded or produced by phylogenetically diverse bacteria are made whenever possible to put these compounds into a larger perspective.
Insights
This review details three post-translationally modified microcins (microcin J25, B17, and C7-C51) from Escherichia coli. These low-molecular-weight antibacterial peptides target essential cellular machinery, offering insights into bacterial defense mechanisms.
Area of Science:
- Microbiology
- Biochemistry
- Molecular Biology
Background:
- Microcins are ribosomally synthesized antibacterial peptides produced by Enterobacteriaceae.
- Some microcins undergo post-translational modification by dedicated enzymes, affecting their activity.
- Low-molecular-weight, modified microcins target essential intracellular molecular machines.
Purpose of the Study:
- To review available structural and functional data on three specific microcins: microcin J25, microcin B17, and microcin C7-C51.
- To discuss the characteristics of these low-molecular-weight, post-translationally modified microcins.
- To place these microcins within a broader context by comparing them to similar peptides from diverse bacterial species.
Main Methods:
- Literature review of structural and functional data.
- Comparative analysis of sequence and structural similarities.
- Inferences based on phylogenetic diversity of producing bacteria.
Main Results:
- Detailed discussion of microcin J25, microcin B17, and microcin C7-C51 structures and functions.
- Identification of these three microcins as low-molecular-weight, post-translationally modified antibacterial peptides.
- Exploration of potential broader roles and origins of these microcin classes.
Conclusions:
- Post-translationally modified microcins represent a significant class of antibacterial agents with diverse structures and targets.
- Comparative analysis aids in understanding the evolution and distribution of microcin systems.
- Further research into these microcins can inform the development of novel antimicrobial strategies.
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