Use of a scaffold peptide in the biosynthesis of amino acid–derived natural products

Author:

Ting Chi P.1ORCID,Funk Michael A.2ORCID,Halaby Steve L.34ORCID,Zhang Zhengan2ORCID,Gonen Tamir34ORCID,van der Donk Wilfred A.125ORCID

Affiliation:

1. Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.

2. Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL, USA.

3. Howard Hughes Medical Institute, University of California, Los Angeles, Los Angeles CA 90095, USA.

4. Departments of Biological Chemistry and Physiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles CA 90095, USA.

5. Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, IL, USA.

Abstract

Growing independently Bacteria produce natural products with a range of functions. A major family comprises ribosomally synthesized and posttranslationally modified peptides. Ting et al. identify a biosynthetic pathway in which a natural product is derived from an amino acid that is added to a ribosomally synthesized peptide independent of the ribosome. This biosynthetic paradigm is used in the synthesis of thiaglutamate and ammosamides, and the finding of related gene clusters suggests that the strategy may be used more widely. Science , this issue p. 280

Funder

Foundation for the National Institutes of Health

Howard Hughes Medical Institute

National Institute of General Medical Sciences

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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