Change search
ReferencesLink to record
Permanent link

Direct link
Enterococcal sex pheromones: evolutionary pathways to complex, two-signal systems
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.ORCID iD: 0000-0001-6848-322X
2016 (English)In: Journal of Bacteriology, ISSN 0021-9193, E-ISSN 1098-5530, Vol. 198, no 11, 1556-1562 p.Article, review/survey (Refereed) Published
Abstract [en]

Gram-positive bacteria carry out intercellular communication using secreted peptides. Important examples of this type of communication are the enterococcal sex pheromone systems, in which the transfer of conjugative plasmids is controlled by intercellular signaling among populations of donors and recipients. This review focuses on the pheromone response system of the conjugative plasmid pCF10. The peptide pheromones regulating pCF10 transfer act by modulating the ability of the PrgX transcription factor to repress the transcription of an operon encoding conjugation functions. Many Gram-positive bacteria regulate important processes, including the production of virulence factors, biofilm formation, sporulation, and genetic exchange using peptide-mediated signaling systems. The key master regulators of these systems comprise the RRNPP (RggRap/NprR/PlcR/PrgX) family of intracellular peptide receptors; these regulators show conserved structures. While many RRNPP systems include a core module of two linked genes encoding the regulatory protein and its cognate signaling peptide, the enterococcal sex pheromone plasmids have evolved to a complex system that also recognizes a second host-encoded signaling peptide. Additional regulatory genes not found in most RRNPP systems also modulate signal production and signal import in the enterococcal pheromone plasmids. This review summarizes several structural studies that cumulatively demonstrate that the ability of three pCF10 regulatory proteins to recognize the same 7-amino-acid pheromone peptide arose by convergent evolution of unrelated proteins from different families. We also focus on the selective pressures and structure/function constraints that have driven the evolution of pCF10 from a simple, single-peptide system resembling current RRNPPs in other bacteria to the current complex inducible plasmid transfer system.

Place, publisher, year, edition, pages
2016. Vol. 198, no 11, 1556-1562 p.
National Category
Structural Biology Evolutionary Biology
URN: urn:nbn:se:umu:diva-119242DOI: 10.1128/JB.00128-16ISI: 000376206300003PubMedID: 27021562OAI: diva2:919790
Available from: 2016-04-15 Created: 2016-04-15 Last updated: 2016-09-28Bibliographically approved

Open Access in DiVA

fulltext(2378 kB)12 downloads
File information
File name FULLTEXT01.pdfFile size 2378 kBChecksum SHA-512
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Berntsson, Ronnie Per-Arne
By organisation
Department of Medical Biochemistry and Biophysics
In the same journal
Journal of Bacteriology
Structural BiologyEvolutionary Biology

Search outside of DiVA

GoogleGoogle Scholar
Total: 12 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 5 hits
ReferencesLink to record
Permanent link

Direct link