Coevolution of the bacterial pheromone ComS and sensor ComR fine-tunes natural transformation in streptococci
| Autor: | Denis Dereinne, Patrice Soumillion, Sylvie Nessler, Johann Mignolet, Felipe Viela, Laura Ledesma-Garcia, Pascal Hols, Yves F. Dufrêne, Imke Ensinck |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Cell signaling Genome evolution DNA transformation competence Mutagenesis (molecular biology technique) Helix-turn-helix Computational biology PcomS comS promoter Biochemistry CAP helix capping helix α16 Pheromones (R)RNPP (Rgg ) Rap NprR PlcR and PrgX Evolution Molecular pheromone XIP SigX-inducing peptide Bacterial Proteins Protein Domains cell signaling Streptococcus thermophilus ComRSth Streptococcus thermophilus ComR XIPSve Streptococcus vestibularis XIP Molecular Biology TPR tetratricopeptide repeat Mechanism (biology) Chemistry ComRSve Streptococcus vestibularis ComR cell-to-cell communication Quorum Sensing streptococcus RLU relative light unit Cell Biology HTH helix-turn-helix XIPSth Streptococcus thermophilus XIP Gene Expression Regulation Bacterial CSP competence-stimulating peptide AFM atomic force microscopy Transformation (genetics) Quorum sensing Tetratricopeptide (R)RNPP XIP FP fluorescence polarization Transformation Bacterial Research Article |
| Zdroj: | The Journal of Biological Chemistry |
| ISSN: | 1083-351X 0021-9258 |
| Popis: | Competence for natural transformation extensively contributes to genome evolution and the rapid adaptability of bacteria dwelling in challenging environments. In most streptococci, this process is tightly controlled by the ComRS signaling system, which is activated through the direct interaction between the (R)RNPP-type ComR sensor and XIP pheromone (mature ComS). The overall mechanism of activation and the basis of pheromone selectivity have been previously reported in Gram-positive salivarius streptococci; however, detailed 3D-remodeling of ComR leading up to its activation remains only partially understood. Here, we identified using a semi-rational mutagenesis approach two residues in the pheromone XIP that bolster ComR sensor activation by interacting with two aromatic residues of its XIP-binding pocket. Random and targeted mutagenesis of ComR revealed that the interplay between these four residues remodel a network of aromatic-aromatic interactions involved in relaxing the sequestration of the DNA-binding domain. Based on these data, we propose a comprehensive model for ComR activation based on two major conformational changes of the XIP-binding domain. Notably, the stimulation of this newly identified trigger point by a single XIP substitution resulted in higher competence and enhanced transformability, suggesting that pheromone-sensor co-evolution counter-selects for hyperactive systems in order to maintain a trade-off between competence and bacterial fitness. Overall, this study sheds new light on the ComRS activation mechanism and how it could be exploited for biotechnological and biomedical purposes. |
| Databáze: | OpenAIRE |
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