Format

Send to:

Choose Destination
See comment in PubMed Commons below
Org Biomol Chem. 2007 Feb 21;5(4):593-602. Epub 2006 Dec 21.

Robust platform for de novo production of heterologous polyketides and nonribosomal peptides in Escherichia coli.

Author information

  • 1Department of Pharmaceutical Sciences, University of Southern California, 1985 Zonal Ave PSC 718, Los Angeles, California 90033, USA. kenjiwat@usc.edu

Erratum in

  • Org Biomol Chem. 2007 Apr 7;5(7):1118.

Abstract

During the past decade, numerous gene clusters responsible for the biosynthesis of important natural products have been identified from a variety of organisms. Heterologous expression utilizing E. coli has been employed to provide proteins for mechanistic understanding and structural analyses. It was very recently shown that this system is also capable of de novo production of biologically active forms of heterologous nonribosomal peptides, echinomycin and triostin A, through the introduction of genes encoding modules responsible for their assembly into this model bacterial host. The superlative advantage of using E. coli as a heterologous host is the availability of a wealth of well-established molecular biological techniques for its genetic and metabolic manipulation. The platform described above which was developed in our laboratory is ideal for use in the production of metabolites found in marine and symbiotic bacteria that are not amenable to artificial cultivation. Development and tailoring of our system will allow for the design of these natural products and ultimately combinatorial yet rational modification of these compounds. This review focuses on the heterologous expression of biosynthetic gene clusters for the assembly of therapeutically potent compounds.

PMID:
17285165
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Royal Society of Chemistry
    Loading ...
    Write to the Help Desk