Abstract
SapB is a morphogenetic peptide that is important for aerial mycelium formation by the filamentous bacterium Streptomyces coelicolor. Production of SapB commences during aerial mycelium formation and depends on most of the genes known to be required for the morphogenesis of aerial hyphae. Furthermore, the application of purified SapB to mutants blocked in morphogenesis restores their capacity to form aerial hyphae. Here, we present evidence that SapB is a lantibiotic-like peptide that is derived by posttranslational modification from the product of a gene (ramS) in the four-gene ram operon, which is under the control of the regulatory gene ramR. We show that the product of another gene in the operon (ramC) contains a region that is similar to enzymes involved in the biosynthesis of lantibiotics, suggesting that it might be involved in the posttranslational processing of RamS. We conclude that SapB is derived from RamS through proteolytic cleavage and the introduction of four dehydroalanine residues and two lanthionine bridges. We provide an example of a morphogenetic role for an antibiotic-like molecule.
MeSH Terms
Amino Acid Sequence
Bacterial Proteins/chemistry,genetics,metabolism
Gene Expression Regulation, Bacterial
Gene Expression Regulation, Developmental
Hydrophobic and Hydrophilic Interactions
Ligases/chemistry,metabolism
Models, Molecular
Molecular Sequence Data
Protein Structure, Tertiary
Streptomyces/genetics,metabolism
Chemicals
Bacterial Proteins
Streptomyces spore-associated proteins
Ligases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Kodani Shinya
Department of Biology, Hofstra University, Hempstead, NY 11549, USA.
Hudson Michael E
Durrant Marcus C
Buttner Mark J
Nodwell Justin R
Willey Joanne M
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