Extracellular proteolysis of tandemly duplicated pheromone propeptides affords additional complexity to bacterial quorum sensing
File(s)
Published version
Author(s)
Type
Journal Article
Abstract
Bacterial interactions are vital for adapting to changing environments, with quorum sensing (QS) systems playing a central role in coordinating behaviors through small signaling molecules. The RRNPPA family is the prevalent QS systems in Bacillota and mediating communication through secreted oligopeptides, which are processed into active pheromones by extracellular proteases. Notably, in several cases the propeptides show the presence of multiple putative pheromones within their sequences, which has been proposed as a mechanism to diversify peptide-receptor specificity and potentially facilitate new functions. However, neither the processes governing the maturation of propeptides containing multiple pheromones, nor their functional significance has been evaluated. Here, using 2 Rap systems from bacteriophages infecting Bacillus subtilis that exhibit different types of pheromone duplication in their propeptides, we investigate the maturation process and the molecular and functional activities of the produced pheromones. Our results reveal that distinct maturation processes generate multiple mature pheromones, which bind to receptors with varying affinities but produce identical structural and biological responses. These findings add additional layers in the complexity of QS communication and regulation, opening new possibilities for microbial social behaviors, highlighting the intricate nature of bacterial interactions and adaptation.
Editor(s)
Stock, Ann M
Date Issued
2024-08-13
Date Acceptance
2024-07-09
Citation
PLoS Biology, 2024, 22 (8)
ISSN
1544-9173
Publisher
Public Library of Science (PLoS)
Journal / Book Title
PLoS Biology
Volume
22
Issue
8
Copyright Statement
© 2024 Felipe-Ruiz et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
License URL
Identifier
https://www.ncbi.nlm.nih.gov/pubmed/39137235
PII: PBIOLOGY-D-24-00993
Subjects
BACILLUS-SUBTILIS
BINDING
Biochemistry & Molecular Biology
Biology
COMPETENCE
DEGU
FAMILY
GENES
Life Sciences & Biomedicine
Life Sciences & Biomedicine - Other Topics
PEPTIDE
PHOSPHATASES
Science & Technology
Publication Status
Published
Coverage Spatial
United States
Article Number
e3002744
Date Publish Online
2024-08-13