Title of article :
In Vivo and In Vitro Trans-Acylation by BryP, the Putative Bryostatin Pathway Acyltransferase Derived from an Uncultured Marine Symbiont Original Research Article
Author/Authors :
Nicole B. Lopanik، نويسنده , , Jennifer A. Shields، نويسنده , , Tonia J. Buchholz، نويسنده , , Christopher M. Rath، نويسنده , , Joanne Hothersall، نويسنده , , Margo G. Haygood، نويسنده , , Kristina H?kansson، نويسنده , , Christopher M. Thomas، نويسنده , , David H. Sherman، نويسنده ,
Issue Information :
ماهنامه با شماره پیاپی سال 2008
Pages :
12
From page :
1175
To page :
1186
Abstract :
The putative modular polyketide synthase (PKS) that prescribes biosynthesis of the bryostatin natural products from the uncultured bacterial symbiont of the marine bryozoan Bugula neritina possesses a discrete open reading frame (ORF) (bryP) that encodes a protein containing tandem acyltransferase (AT) domains upstream of the PKS ORFs. BryP is hypothesized to catalyze in trans acylation of the PKS modules for polyketide chain elongation. To verify conservation of function, bryP was introduced into AT-deletion mutant strains of a heterologous host containing a PKS cluster with similar architecture, and polyketide production was partially rescued. Biochemical characterization demonstrated that BryP catalyzes selective malonyl-CoA acylation of native and heterologous acyl carrier proteins and complete PKS modules in vitro. The results support the hypothesis that BryP loads malonyl-CoA onto Bry PKS modules, and provide the first biochemical evidence of the functionality of the bry cluster.
Journal title :
Chemistry and Biology
Serial Year :
2008
Journal title :
Chemistry and Biology
Record number :
1159620
Link To Document :
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