SapT, a lanthionine-containing peptide involved in aerial hyphae formation in the streptomycetes

Kodani, Shinya, Lodato, Michael, Durrant, Marcus, Picart, Francis and Willey, Joanne (2005) SapT, a lanthionine-containing peptide involved in aerial hyphae formation in the streptomycetes. Molecular Microbiology, 58 (5). pp. 1368-1380. ISSN 0950-382X

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The developmentally complex soil microbe Streptomyces tendae secretes a hydrophobic peptide that restored to developmental mutants of S. coelicolor the ability to raise aerial hyphae. The S. tendae peptide, SapT, has a lantibiotic structure and molecular modelling predicts that it is amphiphilic, making it structurally and functionally similar to the SapB peptide produced by S. coelicolor. However, SapT, which bears three β-methyl lanthionine bridges and one lanthionine bridge and demonstrated limited antibiotic activity, is distinct from SapB. The amphiphilic nature of both SapT and SapB is required for their ability to serve as biosurfactants facilitating the emergence of newly formed aerial hyphae. Remarkably, SapB and SapT, and the fungal hydrophobin SC3 were shown to restore to a SapB-deficient S. coelicolor mutant the capacity to undergo complete morphogenesis, such that the extracellular addition of protein resulted in sporulation. This suggests that the initiation of aerial growth may also indirectly trigger the signal transduction events needed for differentiation. These data imply that the production of morphogenetic peptides may be common among the streptomycetes, but that while their ability to function as biosurfactants is conserved, their specific lantibiotic structure is not. Finally, the identification of a second lanthionine-containing morphogenetic peptide suggests that lantibiotic structure and function may be more diverse than previously thought.

Item Type: Article
Subjects: C500 Microbiology
Department: Faculties > Health and Life Sciences > Applied Sciences
Depositing User: Becky Skoyles
Date Deposited: 03 Feb 2015 10:01
Last Modified: 12 Oct 2019 17:30

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