title: An expanding universe of small proteins.
abstract: Historically, small proteins (sproteins) of less than 50 amino acids, in their final processed forms or genetically encoded as such, have been understudied. However, both serendipity and more recent focused efforts have led to the identification of a number of new sproteins in both Gram-negative and Gram-positive bacteria. Increasing evidence demonstrates that sproteins participate in a wide array of cellular processes and exhibit great diversity in their mechanisms of action, yet general principles of sprotein function are emerging. This review highlights examples of sproteins that participate in cell signaling, act as antibiotics and toxins, and serve as structural proteins. We also describe roles for sproteins in detecting and altering membrane features, acting as chaperones, and regulating the functions of larger proteins.
authors.affiliation: Cell Biology and Metabolism Program, NICHD, Building 18T, Room 101, 18 Library Dr MSC 5430, National Institutes of Health, Bethesda, MD 20892-5430, USA.
authors.forename: Errett C
authors.initials: EC
authors.lastname: Hobbs
authors.forename: Fanette
authors.initials: F
authors.lastname: Fontaine
authors.forename: Xuefeng
authors.initials: X
authors.lastname: Yin
authors.forename: Gisela
authors.initials: G
authors.lastname: Storz
mesh_terms: D023181:Antimicrobial Cationic Peptides / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D001427:Bacterial Toxins / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D006090:Gram-Negative Bacteria / Q000378:metabolism*; D006094:Gram-Positive Bacteria / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D008565:Membrane Proteins; D018832:Molecular Chaperones