Genetic and Structural Analyses of RRNPP Intercellular Peptide Signaling of Gram-Positive Bacteria

Author:

Neiditch Matthew B.1,Capodagli Glenn C.1,Prehna Gerd2,Federle Michael J.3

Affiliation:

1. Department of Microbiology, Biochemistry, and Molecular Genetics, New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, New Jersey 07103, USA;,

2. Center for Structural Biology, Research Resources Center and Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, Illinois 60607, USA;

3. Department of Medicinal Chemistry and Pharmacognosy and Center for Biomolecular Sciences, University of Illinois at Chicago, Chicago, Illinois 60607, USA;

Abstract

Bacteria use diffusible chemical messengers, termed pheromones, to coordinate gene expression and behavior among cells in a community by a process known as quorum sensing. Pheromones of many gram-positive bacteria, such as Bacillus and Streptococcus, are small, linear peptides secreted from cells and subsequently detected by sensory receptors such as those belonging to the large family of RRNPP proteins. These proteins are cytoplasmic pheromone receptors sharing a structurally similar pheromone-binding domain that functions allosterically to regulate receptor activity. X-ray crystal structures of prototypical RRNPP members have provided atomic-level insights into their mechanism and regulation by pheromones. This review provides an overview of RRNPP prototype signaling; describes the structure–function of this protein family, which is spread widely among gram-positive bacteria; and suggests approaches to target RRNPP systems in order to manipulate beneficial and harmful bacterial behaviors.

Publisher

Annual Reviews

Subject

Genetics

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