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Activation and identification of five clusters for secondary metabolites in Streptomyces albus J1074
A cluster for glycosylated compounds (paulomycins) was also identified by comparison of the high‐performance liquid chromatography profiles of the wild‐type strain with that of a mutant in which two key enzymes of the cluster were simultaneously deleted.
Minimum Information about a Biosynthetic Gene cluster.
This work proposes the Minimum Information about a Biosynthetic Gene cluster (MIBiG) data standard, to facilitate consistent and systematic deposition and retrieval of data on biosynthetic gene clusters.
The formation of the rodlet layer of streptomycetes is the result of the interplay between rodlins and chaplins
Evidence is presented that rodlet formation is conserved in the streptomycetes, and expression per aerial hypha was similar to that in the wild‐type strain, indicating that expression of the rdl genes is initiated after the hypha has sensed that it has grown into the air.
Combinatorial biosynthesis of antitumor indolocarbazole compounds.
- C. Sánchez, Lili Zhu, J. Salas
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 11 January 2005
A biological process based on combinatorial biosynthesis for the production of indolocarbazole compounds (or their precursors) in engineered microorganisms as a complementary approach to chemical synthesis is reported.
Mithramycin SK, a novel antitumor drug with improved therapeutic index, mithramycin SA, and demycarosyl-mithramycin SK: three new products generated in the mithramycin producer Streptomyces…
- L. Remsing, A. González, J. Rohr
- Biology, ChemistryJournal of the American Chemical Society
- 14 May 2003
The structures of these three compounds confirmed indirectly the proposed role of MtmW in MTM biosynthesis, and the new mithramycin derivatives bear unexpectedly shorter 3-side chains than MTM, presumably caused by nonenzymatic rearrangement or cleavage reactions of the initially formed pentyl side chain with a reactive beta-dicarbonyl functional group.
Two glycosyltransferases and a glycosidase are involved in oleandomycin modification during its biosynthesis by Streptomyces antibioticus
- L. Quirós, I. Aguirrezabalaga, C. Olano, C. Méndez, J. Salas
- Biology, ChemistryMolecular microbiology
- 1 June 1998
A model is proposed integrating these and previously reported results for intracellular inactivation, secretion and extracellular reactivation of oleandomycin, with OleI being much more specific for ole fandomycin.
Interspecies complementation in Saccharopolyspora erythraea : elucidation of the function of oleP1, oleG1 and oleG2 from the oleandomycin biosynthetic gene cluster of Streptomyces antibioticus and…
- M. Doumith, R. Legrand, Catherine Lang, J. Salas, M. Raynal
- Biology, ChemistryMolecular microbiology
- 1 December 1999
Interspecies complementation has been carried out, using two mutant strains of Saccharopolyspora erythraea to identify which of these two glycosyltransferases encodes the desosaminyltransferase and which the oleandrosyltransferase, and to demonstrate that the function of OleP1 is identical to that of EryCII in the biosynthesis of dTDP‐d‐desosamine.
Production, purification and partial characterization of two extracellular proteases from Serratia marcescens grown in whey
Fine structure, physiology and biochemistry of arthrospore germination in Streptomyces antibioticus.
- C. Hardisson, M. Manzanal, J. Salas, J. Suárez
- Biology, MedicineJournal of general microbiology
- 1 April 1978
During germination, Streptomyces antibioticus arthrospores passed through stages: darkening, swelling and germ tube emergence, where the spores exhibited the highest cytochrome oxidase and catalase activities and respiratory quotient.
A second ABC transporter is involved in oleandomycin resistance and its secretion by Streptomyces antibioticus
Functional analysis of the oleB gene showed that either the first or the second half of the gene containing only one ATP‐binding domain was sufficient to confer resistance to oleandomycin, and it was shown that a Streptomyces albus strain, containing both a glycosyltransferase and the OleB protein, was capable ofglycosylating ole fandomycin and secreting the inactive Glycosylated molecule.