The hidden diversity of ribosomal peptide natural products

Abstract

A recent report in BMC Biology on the discovery and analysis of biosynthetic genes for ribosomal peptide natural products confirms that these pathways are much more common and diverse than previously suspected, contributing substantially to the chemical arsenal employed by bacteria. See research article http://www.biomedcentral.com/1741-7007/8/70.

Figure 1

Diversity in ribosomal peptide natural products is produced by variety in enzymatic modification and precursor peptide hypervariability. (a) Although precursor peptides consist of many different apparently unrelated sequence groups, in general they contain a relatively conserved leader sequence directing enzyme modification (grey) and a hypervariable core sequence that encodes the final natural product (red). (b) In this study [1] cyclodehydrating and lanthionine-bond forming enzymes were analyzed, but other modifying enzymes exist, leading to numerous posttranslational modifications. (c) Further derivatization by multiple types of enzymes, including proteases that cleave the peptide product from the leader peptide, add to the chemical diversity of ribosomal peptide natural products.