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AmfS, an extracellular peptidic morphogen in Streptomyces griseus.


ABSTRACT: The amf gene cluster was previously identified as a regulator for the onset of aerial-mycelium formation in Streptomyces griseus. The nucleotide sequences of amf and its counterparts in other species revealed a conserved gene organization consisting of five open reading frames. A nonsense mutation in amfS, encoding a 43-amino-acid peptide, caused significant blocking of aerial-mycelium formation and streptomycin production, suggesting its role as a regulatory molecule. Extracellular-complementation tests for the aerial-mycelium-deficient phenotype of the amfS mutant demonstrated that AmfS was secreted by the wild-type strain. A null mutation in amfBA, encoding HlyB-like membrane translocators, abolished the extracellular AmfS activity without affecting the wild-type morphology, which suggests that AmfBA is involved not in production but in export of AmfS. A synthetic C-terminal octapeptide partially induced aerial-mycelium formation in the amfS mutant, which suggests that an AmfS derivative, but not AmfS itself, serves as an extracellular morphogen.

SUBMITTER: Ueda K 

PROVIDER: S-EPMC134859 | biostudies-literature | 2002 Mar

REPOSITORIES: biostudies-literature

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AmfS, an extracellular peptidic morphogen in Streptomyces griseus.

Ueda Kenji K   Oinuma Ken-Ichi K   Ikeda Go G   Hosono Kuniaki K   Ohnishi Yasuo Y   Horinouchi Sueharu S   Beppu Teruhiko T  

Journal of bacteriology 20020301 5


The amf gene cluster was previously identified as a regulator for the onset of aerial-mycelium formation in Streptomyces griseus. The nucleotide sequences of amf and its counterparts in other species revealed a conserved gene organization consisting of five open reading frames. A nonsense mutation in amfS, encoding a 43-amino-acid peptide, caused significant blocking of aerial-mycelium formation and streptomycin production, suggesting its role as a regulatory molecule. Extracellular-complementat  ...[more]

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