tylosin-biosynthetic genes of Streptomyces fradiae

The tylosin-biosynthetic (tyl) gene cluster occupies about 1% of the genome of Streptomyces fradiae and includes at least 43 open reading frames. In addition to structural genes required for tylosin production, the tylcluster contains three resistance determinants and several regulatory genes. Tylos...

Full description

Saved in:
Bibliographic Details
Published in:Antonie van Leeuwenhoek 2001-09, Vol.79 (3-4), p.229-234
Main Authors: Cundliffe, Eric, Bate, Neil, Butler, Andrew, Fish, Steven, Gandecha, Atul, Merson-Davies, Louise
Format: Article
Language:English
Subjects:
aglycone
Anti-Bacterial Agents - biosynthesis
Antibiotics (antibacterial agents, antifungal agents)
Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents
Applied microbiology
Bacteria
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacteriology
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
g-Butyrolactone
Gene Expression Regulation, Bacterial
Genes
Genes, Bacterial
Genetics
glycosylation
Microbiology
Multigene Family
open reading frames
polyketide synthase
polyketide synthases
regulator genes
Streptomyces - genetics
Streptomyces - metabolism
Streptomyces fradiae
structural genes
thioesterase
tylosin
Tylosin - biosynthesis
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The tylosin-biosynthetic (tyl) gene cluster occupies about 1% of the genome of Streptomyces fradiae and includes at least 43 open reading frames. In addition to structural genes required for tylosin production, the tylcluster contains three resistance determinants and several regulatory genes. Tylosin production is evidently controlled by pathway-specific and pleiotropic regulators with the likely involvement of γ-butyrolactone signalling factors. Accumulation of the polyketide aglycone is controlled by glycosylated macrolides and optimal performance of the complex polyketide synthase enzyme requires the activity of an editing thioesterase.
ISSN:0003-6072
1572-9699
DOI:10.1023/A:1012065300116