Low-molecular-weight post-translationally modified microcins

Konstantin Severinov; Ekaterina Semenova; Alexey Kazakov; Teymur Kazakov; Mikhail S. Gelfand

doi:10.1111/j.1365-2958.2007.05874.x

Low-molecular-weight post-translationally modified microcins

Konstantin Severinov, Ekaterina Semenova, Alexey Kazakov, Teymur Kazakov, Mikhail S. Gelfand

Rutgers, The State University

Research output: Contribution to journal › Short survey › peer-review

103 Scopus citations

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.

Original language	American English
Pages (from-to)	1380-1394
Number of pages	15
Journal	Molecular Microbiology
Volume	65
Issue number	6
DOIs	https://doi.org/10.1111/j.1365-2958.2007.05874.x
State	Published - Sep 2007

ASJC Scopus subject areas

Microbiology
Molecular Biology

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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.",

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AU - Severinov, Konstantin

AU - Semenova, Ekaterina

AU - Kazakov, Alexey

AU - Kazakov, Teymur

AU - Gelfand, Mikhail S.

PY - 2007/9

Y1 - 2007/9

N2 - 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.

AB - 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.

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Low-molecular-weight post-translationally modified microcins

Abstract

ASJC Scopus subject areas

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