Chemical communication in proteobacteria: biochemical and structural studies of signal synthases and receptors required for intercellular signalling

• Published in: Molecular microbiology 2004-08, Vol.53 (3), p.755-769
• Main Authors: Pappas, Katherine M., Weingart, Christine L., Winans, Stephen C.
• Format: Article
• Language: English
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - physiology; Biological and medical sciences; Carbon-Sulfur Lyases; Cell Communication - physiology; Fundamental and applied biological sciences. Psychology; Ligases - metabolism; Microbiology; Proteobacteria; Proteobacteria - physiology; Repressor Proteins - physiology; Signal Transduction - physiology; Trans-Activators - physiology; Vibrio - physiology; Vibrio fischeri; Vibrio harveyi
• ISSN: 0950-382X; 1365-2958
• DOI: 10.1111/j.1365-2958.2004.04212.x

Summary Cell–cell communication via the production and detection of chemical signal molecules has been the focus of a great deal of research over the past decade. One class of chemical signals widely used by proteobacteria consists of N‐acyl‐homoserine lactones, which are synthesized by proteins related to LuxI of Vibrio fischeri and are detected by proteins related to the V. fischeri LuxR protein. A related marine bacterium, Vibrio harveyi, communicates using two chemical signals, one of which, autoinducer‐2 (AI‐2), is a furanone borate diester that is synthesized by the LuxS protein and detected by a periplasmic protein called LuxP. Evidence from a number of laboratories suggests that AI‐2 may be used as a signal by diverse groups of bacteria, and might permit intergeneric signalling. These two families of signalling systems have been studied from the perspectives of physiology, ecology, biochemistry, and more recently, structural biology. Here, we review the biochemistry and structural biology of both acyl‐homoserine‐lactone‐dependent and AI‐2‐dependent signalling systems.