Open AccessAn 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
Author(s) -
Paitan Yossi,
Orr Elisha,
Ron Eliora Z.,
Rosenberg Eugene
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10840.x
Subject(s) - acyl carrier protein , myxococcus xanthus , polyketide synthase , acyltransferase , biochemistry , atp synthase , biology , biosynthesis , polyketide , hydroxylation , gene , acyltransferases , enzyme , stereochemistry , chemistry , mutant
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.