Microcin J25 has two targets in sensitive bacteria, the RNA polymerase, and the respiratory chain through inhibition of cellular respiration. In this work, the effect of microcin J25 in E. coli mutants that lack the terminal oxidases cytochrome bd-I and cytochrome bo was analyzed. The mutant strains lacking cytochrome bo or cytochrome bd-I were less sensitive to the peptide. In membranes obtained from the strain that only expresses cytochrome bd-I a great ROS overproduction was observed in the presence of microcin J25. Nevertheless, the oxygen consumption was less inhibited in this strain, probably because the oxygen is partially reduced to superoxide. There was no overproduction of ROS in membranes isolated from the mutant strain that only express cytochrome bo and the inhibition of the cellular respiration was similar to the wild type. It is concluded that both cytochromes bd-I and bo are affected by the peptide. The results establish for the first time a relationship between the terminal oxygen reductases and the mechanism of action of microcin J25.
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http://dx.doi.org/10.1016/j.bbabio.2017.10.006 | DOI Listing |
Elife
December 2024
Program in Microbiome Dynamics, University of Massachusetts Chan Medical School, Worcester, United States.
Interspecies interactions involving direct competition bacteriocin production play a vital role in shaping ecological dynamics within microbial ecosystems. For instance, the ribosomally produced siderophore bacteriocins, known as class IIb microcins, affect the colonization of host-associated pathogenic species. Notably, to date, only five of these antimicrobials have been identified, all derived from specific and strains.
View Article and Find Full Text PDFMicrobiol Res
February 2025
Department of Molecular Genetics, University of Groningen, Groningen, Nijenborgh 7, Groningen 9747AG, the Netherlands. Electronic address:
Synechococsins represent a diverse group of class II lanthipeptides from the prochlorosin family, produced by the marine picocyanobacterium Synechococcus. A single strain can produce multiple SyncA peptides through modification by SyncM, a bifunctional lanthipeptide synthetase. Despite the prevalence of these lanthipeptides in nature, their biological functions remain elusive, even for the most studied group, Prochlorococcus MIT9313.
View Article and Find Full Text PDFCell Host Microbe
November 2024
Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA; Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX, USA; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, USA. Electronic address:
Microcins are antibacterial small proteins secreted by gram-negative bacteria. In this issue of Cell Host & Microbe, Kim et al. report the discovery of a V.
View Article and Find Full Text PDFJ Anim Sci Biotechnol
November 2024
State Key Laboratory of Animal Nutrition and Feeding, Ministry of Agriculture and Rural Affairs Feed Industry Centre, China Agricultural University, Beijing, 100193, P.R. China.
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