A cytochrome P450‐like gene possibly involved in oleandomycin biosynthesis by Streptomyces antibioticus

A cosmid clone from an oleandomycin producer, Streptomyces antibioticus, contains a large open reading frame encoding a type I polyketide synthase subunit and an oleandomycin resistance gene (oleB). Sequencing of a 1.4‐kb DNA fragment adjacent to oleB revealed the existence of an open reading frame...

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Bibliographic Details
Published in:FEMS microbiology letters 1995-03, Vol.127 (1‐2), p.117-120
Main Authors: Rodriguez, Ana Maria, Olano, Carlos, Méndez, Carmen, Hutchinson, C. Richard, Salas, JoséA.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - biosynthesis
Bacterial Proteins - genetics
Bacterial Proteins - immunology
Bacteriology
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
Cytochrome P-450 Enzyme System - genetics
Drug Resistance, Microbial - genetics
Epoxidation
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Genes, Bacterial
Genetics
Kinetics
Macrolides
Microbiology
Mission oriented research
Molecular Sequence Data
Multienzyme Complexes - genetics
Oleandomycin - biosynthesis
Open Reading Frames
Oxygenases - genetics
Polyketides
Recombinant DNA
Secondary metabolism
Sequence Homology, Amino Acid
Streptomyces antibioticus
Streptomyces antibioticus - genetics
Streptomyces antibioticus - metabolism
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Summary:A cosmid clone from an oleandomycin producer, Streptomyces antibioticus, contains a large open reading frame encoding a type I polyketide synthase subunit and an oleandomycin resistance gene (oleB). Sequencing of a 1.4‐kb DNA fragment adjacent to oleB revealed the existence of an open reading frame (oleP) encoding a protein similar to several cytochrome P450 monooxygenases from different sources, including the products of the eryF and eryK genes from Saccharopolyspora erythraea that participate in erythromycin biosynthesis. The oleP gene was expressed in Escherichia coli as a fusion protein to a maltose‐binding protein. Using polyclonal antibodies against this fusion protein it was observed that the synthesis of the cytochrome P450 was in parallel to that of oleandomycin. The cytochrome P450 encoded by the oleP gene could be responsible for the epoxidation of carbon 8 of the oleandomycin lactone ring.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1995.tb07459.x