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    Prospecting Genomes For Lasso Peptides: Mikhail O. Maksimov A. James Link

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    Prospecting Genomes For Lasso Peptides: Mikhail O. Maksimov A. James Link

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    Prospecting Genomes For Lasso Peptides: Mikhail O. Maksimov A. James Link

    Uploaded by

    Venkata Suryanarayana Gorle
    fe

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
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    J Ind Microbiol Biotechnol (2014) 41:333344

    DOI 10.1007/s10295-013-1357-4

    REVIEW

    Prospecting genomes forlasso peptides


    MikhailO.Maksimov A.JamesLink

    Received: 4 August 2013 / Accepted: 23 September 2013 / Published online: 19 October 2013
    Society for Industrial Microbiology and Biotechnology 2013

    Abstract Genome mining has unlocked a veritable treasure chest of natural compounds. However, each family of
    natural products requires a genome-mining approach tailored to its unique features to be successful. Lasso peptides
    are ribosomally synthesized and posttranslationally modified products with a unique three-dimensional structure.
    Advances in the understanding of these molecules have
    informed the design of strategies to identify new members
    of the class in sequenced genomes. This review presents
    the bioinformatic methods used to discover novel lasso
    peptides and describes how such analyses have afforded
    insights into the biosynthesis and evolution of this peptide
    class.
    Keywords Lasso peptides RiPPs Genome mining

    Introduction
    With the advent of abundant, freely available genome
    sequences, the field of natural products discovery has been
    transformed. The chemistry that endows natural products
    with their beautiful and complex structures is increasingly
    being mapped to specific genes [43]. A related activity,
    genome mining, involves searching genomes for genes or
    gene clusters indicative of natural product biosynthesis.
    A milestone in these genomics-based approaches for the
    M.O.Maksimov A.J.Link(*)
    207 Hoyt Laboratory, Department ofChemical andBiological
    Engineering, Princeton University, Princeton, NJ 08544, USA
    e-mail: ajlink@princeton.edu
    A.J.Link
    Department ofMolecular Biology, Princeton University,
    Princeton, NJ, USA

    study of natural products is certainly the complete sequencing of the Streptomyces coelicolor genome, carried out by
    a team led by Sir David Hopwood [4]. In the decade-plus
    since the S. coelicolor genome was published, genomic
    tools have become requisite additions to the natural products researchers toolbox. In honor of Sir Hopwoods 80th
    birthday this year and his myriad contributions to natural
    products research, this article will describe how genomemining approaches have been used to increase our understanding of lasso peptides, a class of ribosomally derived
    naturally products.
    Lasso peptides belong to a large and ever-growing superfamily of natural products arising from ribosomally synthesized polypeptide precursors. This superfamily has recently
    been given the moniker RiPPs for ribosomally synthesized
    and posttranslationally modified peptides [1]. RiPPs lend
    themselves especially to genomemining approaches [41]
    because of the gene-encoded nature of their precursors.
    Many RiPPs include extensive posttranslational modifications [10] including chemical moieties reminiscent of modifications generated by non-ribosomal peptide synthetase
    (NRPS) tailoring enzymes [29]. In contrast to heavily modified RiPPs such as cyanobactins [8] and bottromycins [15]
    that look little like their ribosomally synthesized precursors, lasso peptides are relatively bereft of posttranslational
    modifications. However, lasso peptides do fold into a truly
    remarkable right-handed, threaded three-dimensional structure reminiscent of a slipknot or lasso (Fig.1). This structure is held together by a single posttranslationally installed
    isopeptide bond that joins the N-terminus of the matured
    peptide to a glutamate or aspartate sidechain eight or nine
    amino acids down the chain. The C-terminal portion of
    the peptide, ranging from 7 to 15 amino acids, is threaded
    through this ring resulting in the lasso structure. Diversity
    in the lasso peptide family comes from the wide variety of

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