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pubmed-article:11583847pubmed:abstractTextThe antibiotic TA of Myxococcus xanthus is produced by a type-I polyketide synthase mechanism. Previous studies have indicated that TA genes are clustered within a 36-kb region. The chemical structure of TA indicates the need for several post-modification steps, which are introduced to form the final bioactive molecule. These include three C-methylations, an O-methylation and a specific hydroxylation. In this study, we describe the genetic analysis of taK, encoding a specific polyketide beta-ketoacyl:acyl carrier protein synthase, which contains an unusual beta-ketoacyl synthase and acyltransferase motifs and is likely to be involved in antibiotic TA post-modification. Functional analysis of this beta-ketoacyl:acyl carrier protein synthase by specific gene disruption suggests that it is essential for the production of an active TA molecule.lld:pubmed
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pubmed-article:11583847pubmed:pagination191-7lld:pubmed
pubmed-article:11583847pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:11583847pubmed:articleTitleAn unusual beta-ketoacyl:acyl carrier protein synthase and acyltransferase motifs in TaK, a putative protein required for biosynthesis of the antibiotic TA in Myxococcus xanthus.lld:pubmed
pubmed-article:11583847pubmed:affiliationDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, Israel.lld:pubmed
pubmed-article:11583847pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11583847pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed