Hydrophobic peptides: novel regulators within bacterial membrane.
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.
Alix
Eric
E
Inserm, ESPRI 26, Avenue J. F. Kennedy, 30908 Nîmes cedex 02, France.
Blanc-Potard
Anne-Béatrice
AB
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D016366:Open Reading Frames; D010455:Peptides / Q000235:genetics / Q000378:metabolism*; D017433:Protein Structure, Secondary; D012486:Salmonella typhimurium / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D008565:Membrane Proteins; D010455:Peptides