Hydrophobic peptides: novel regulators within bacterial membrane

• Published in: Molecular microbiology Vol. 72; no. 1; pp. 5 - 11
• Main Authors: Alix, Eric, Blanc-Potard, Anne-Béatrice
• Format: Journal Article
• Language: English
• Published: Oxford, UK Oxford, UK : Blackwell Publishing Ltd 01.04.2009; Blackwell Publishing Ltd; Blackwell; Wiley
• Subjects: Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacteriology; Biological and medical sciences; E coli; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Fundamental and applied biological sciences. Psychology; Hydrophobic and Hydrophilic Interactions; Life Sciences; Membrane Proteins - genetics; Membrane Proteins - metabolism; Membranes; Microbiology; Miscellaneous; Molecular biology; Open Reading Frames; Peptides; Peptides - genetics; Peptides - metabolism; Protein Structure, Secondary; Salmonella; Salmonella enterica; Salmonella typhimurium - genetics; Salmonella typhimurium - metabolism; Microbiology; Peptides; Bacteria
• ISSN: 0950-382X; 1365-2958
• DOI: 10.1111/j.1365-2958.2009.06626.x

Identification of short coding sequences is challenging, both experimentally and in silico, and functional natural peptides (< 50 amino acids) have to a large extent been overlooked in Gram-negative bacteria. Recent results have converged to highlight the role of hydrophobic peptides that form a novel class of active molecules in Escherichia coli and Salmonella enterica serovar Typhimurium. These peptides can play a regulatory role by interacting with protein partners at the inner membrane and by modulating protein partner activity or stability. Genome-wide analyses in both bacterial species have identified several conserved short open reading frames encoding a single transmembrane segment. We discuss the known and predicted membrane-associated peptides and the tools for their identification. Besides the identification of novel regulatory networks, characterization of peptides with a single transmembrane helix segment and proteins that interact with them provides a powerful opportunity to study interactions between alpha helices within biological membranes. In addition, some bioactive membrane peptides could provide a basis for engineering membrane protein antagonists.