An unusual β-ketoacyl:acyl carrier protein synthase and acyltransferase motifs in taK, a putative protein required for biosynthesis of the antibiotic TA in Myxococcus xanthus

Yossi Paitan, Elisha Orr, Eliora Z. Ron, Eugene Rosenberg*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The 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 β-ketoacyl:acyl carrier protein synthase, which contains an unusual β-ketoacyl synthase and acyltransferase motifs and is likely to be involved in antibiotic TA post-modification. Functional analysis of this β-ketoacyl:acyl carrier protein synthase by specific gene disruption suggests that it is essential for the production of an active TA molecule.

Original languageEnglish
Pages (from-to)191-197
Number of pages7
JournalFEMS Microbiology Letters
Volume203
Issue number2
DOIs
StatePublished - 25 Sep 2001

Funding

FundersFunder number
Cancer Research Campaign
Morris and Manja Leigh Chair for Biophsics and Biotechnology
Federation of European Microbiological Societies

    Keywords

    • Antibiotic biosynthesis
    • Myxococcus xanthus
    • Polyketide synthase
    • Polyketides post-modification
    • β-Ketoacyl synthase
    • β-Ketoacyl:ACP synthase

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