SapB and the chaplins: connections between morphogenetic proteins in Streptomyces coelicolor.
Morphogenesis in the streptomycetes features the differentiation of substrate-associated vegetative hyphae into upwardly growing aerial filaments. This transition requires the activity of bld genes and the secretion of biosurfactants that reduce the surface tension at the colony-air interface enabling the emergence of nascent aerial hyphae. Streptomyces coelicolor produces two classes of surface-active molecules, SapB and the chaplins. While both molecules are important for aerial development, nothing is known about the functional redundancy or interaction of these surfactants apart from the observation that aerial hyphae formation can proceed via one of two pathways: a SapB-dependent pathway when cells are grown on rich medium and a SapB-independent pathway on poorly utilized carbon sources such as mannitol. We used mutant analysis to show that while the chaplins are important, but not required, for development on rich medium, they are essential for differentiation on MS (soy flour mannitol) medium, and the corresponding developmental defects could be suppressed by the presence of SapB. Furthermore, the chaplins are produced by conditional bld mutants during aerial hyphae formation when grown on the permissive medium, MS, suggesting that the previously uncharacterized SapB-independent pathway is chaplin dependent. In contrast, a bld mutant blocked in aerial morphogenesis on all media makes neither SapB nor chaplins. Finally, we show that a constructed null mutant that lacks all chaplin and SapB biosynthetic genes fails to differentiate in any growth condition. We propose that the biosurfactant activities of both SapB and the chaplins are essential for normal aerial hyphae formation on rich medium, while chaplin biosynthesis and secretion alone drives aerial morphogenesis on MS medium.
Capstick
David S
DS
Department of Biology, McMaster University, Hamilton, Ontario L8S4K1, Canada.
Willey
Joanne M
JM
Buttner
Mark J
MJ
Elliot
Marie A
MA
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D003470:Culture Media / Q000494:pharmacology; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D017353:Gene Deletion; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects; D015151:Immunoblotting; D008353:Mannitol / Q000494:pharmacology; D009154:Mutation; D010641:Phenotype; D010957:Plasmids / Q000235:genetics; D015398:Signal Transduction / Q000235:genetics / Q000502:physiology; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D048372:Streptomyces coelicolor / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism / Q000502:physiology
D001426:Bacterial Proteins; D003470:Culture Media; D004268:DNA-Binding Proteins; C087736:RamR protein, Streptomyces; C055447:Streptomyces spore-associated proteins; D014157:Transcription Factors; D008353:Mannitol