The SapB morphogen is a lantibiotic-like peptide derived from the product of the developmental gene ramS in Streptomyces coelicolor

Kodani, Shinya, Durrant, Marcus, Hudson, Michael, Buttner, Mark, Nodwell, Justin and Willey, Joanne (2004) The SapB morphogen is a lantibiotic-like peptide derived from the product of the developmental gene ramS in Streptomyces coelicolor. Proceedings of the National Academy of Sciences of the United States of America, 101 (31). pp. 11448-11453. ISSN 0027-8424

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Official URL: http://dx.doi.org/10.1073/pnas.0404220101

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.

Item Type: Article
Additional Information: This paper deals with how a model bacterium propagates itself by the release of spores from hyphae. Durrant's contribution was to develop a 3D model for one of the key peptides involved in this process, allowing for an interpretation of the experimental data at an atomic level.
Subjects: A100 Pre-clinical Medicine
Department: Faculties > Health and Life Sciences > School of Life Sciences > Applied Sciences
Depositing User: EPrints Services
Date Deposited: 22 Dec 2008 12:32
Last Modified: 07 Mar 2016 14:37
URI: http://nrl.northumbria.ac.uk/id/eprint/1716

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