A molecular key for building hyphae aggregates: the role of the newly identified Streptomyces protein HyaS

Autor(en): Koebsch, Ilona
Overbeck, Jens
Piepmeyer, Sophie
Meschke, Holger
Schrempf, Hildgund 
Stichwörter: Biotechnology & Applied Microbiology; Microbiology
Erscheinungsdatum: 2009
Volumen: 2
Ausgabe: 3
Startseite: 343
Seitenende: 360
Streptomycetes produce many metabolites with medical and biotechnological applications. During fermentations, their hyphae build aggregates, a process in which the newly identified protein HyaS plays an important role. The corresponding hyaS gene is present within all investigated Streptomyces species. Reporter fusions indicate that transcription of hyaS occurs within substrate hyphae of the Streptomyces lividans wild type (WT). The HyaS protein is dominantly associated with the substrate hyphae. The WT strain forms cylindrically shaped clumps of densely packed substrate hyphae, often fusing to higher aggregates (pellets), which remain stably associated during shaking. Investigations by electron microscopy suggest that HyaS induces tight fusion-like contacts among substrate hyphae. In contrast, the pellets of the designed hyaS disruption mutant Delta H are irregular in shape, contain frequently outgrowing bunches of hyphae, and fuse less frequently. Delta H complemented with a plasmid carrying hyaS resembles the WT phenotype. Biochemical studies indicate that the C-terminal region of HyaS has amine oxidase activity. Investigations of Delta H transformants, each carrying a specifically mutated gene, lead to the conclusion that the in situ oxidase activity correlates with the pellet-inducing role of HyaS, and depends on the presence of certain histidine residues. Furthermore, the level of undecylprodigiosin, a red pigment with antibiotic activity, is influenced by the engineered hyaS subtype within a strain. These data present the first molecular basis for future manipulation of pellets, and concomitant production of secondary metabolites during biotechnological processes.
ISSN: 17517907
DOI: 10.1111/j.1751-7915.2009.00093.x

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