Metagenome Mining Reveals Polytheonamides as Posttranslationally Modified Ribosomal Peptides-Reference-Cited by-同舟云学术

Metagenome Mining Reveals Polytheonamides as Posttranslationally Modified Ribosomal Peptides

Published:2012-10-19 Issue:6105 Volume:338 Page:387-390
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Freeman Michael F.¹,Gurgui Cristian¹,Helf Maximilian J.¹,Morinaka Brandon I.¹,Uria Agustinus R.¹,Oldham Neil J.²,Sahl Hans-Georg³,Matsunaga Shigeki⁴,Piel Jörn¹⁵

Affiliation:

1. Kekulé Institute of Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn, Germany.

2. School of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK.

3. Institute of Medical Microbiology, Immunology and Parasitology, University of Bonn, Meckenheimer Allee 168, 53115 Bonn, Germany.

4. Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan.

5. Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zurich, Wolfgang-Pauli-Strasse 10, 8093 Zurich, Switzerland.

Abstract

Made and Modified The polytheonamides are 48-residue toxins derived from marine sponges that include 18 D -amino acids, as well as many other unusual amino acid modifications. Given the complexity, one might guess that these peptides are the product of nonribosomal, peptide synthetase (NRPS). However, Freeman et al. (p. 387 , published online 13 September now show that polytheonamides are produced by a bacterial symbiont using a ribosomal pathway. Six candidate enzymes for the 48 posttranslational modifications were identified and three were functionally validated. Such ribosomal systems could be useful in bioengineering.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference34 articles.

1. Polytheonamides A and B, Highly Cytotoxic, Linear Polypeptides with Unprecedented Structural Features, from the Marine Sponge, Theonella swinhoei

2. Solution Structure of Polytheonamide B, a Highly Cytotoxic Nonribosomal Polypeptide from Marine Sponge

3. Total synthesis of the large non-ribosomal peptide polytheonamide B

4. Nonribosomal peptide synthetases: structures and dynamics

5. Follow the leader: the use of leader peptides to guide natural product biosynthesis

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