A novel family of cyclic oligopeptides derived from ribosomal peptide synthesis of an in planta-induced gene, gigA, in Epichloë endophytes of grasses

Johnson, Richard D.; Lane, Geoffrey A.; Koulman, Albert; Cao, Mingshu; Fraser, Karl; Fleetwood, Damien J.; Voisey, Christine R.; Dyer, Jolon M.; Pratt, J.M.; Christensen, Michael J.; Simpson, Wayne R.; Bryan, Gregory T.; Johnson, Linda J.

doi:10.1016/j.fgb.2015.10.005

Cited by 54 publications

(68 citation statements)

References 58 publications

(78 reference statements)

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“…Some repeat-containing proteins contain kexin cleavage sites between the repeating units resulting in generation of bioactive peptides. A classic example of this in Epichloë is GigA, which is processed to generate a series of cyclic peptides called epichloëcyclins of unknown biological function [111]. In U. maydis , Rep1, is processed into smaller peptides that form cell wall associated fibrils mediating attachment of the hyphae to hydrophobic surfaces [112, 113].…”

Section: Discussionmentioning

confidence: 99%

Analysis of Epichloë festucae small secreted proteins in the interaction with Lolium perenne

Scott

Hassing

Winter

et al. 2018

Preprint

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19Epichloë festucae is an endophyte of the agriculturally important perennial 20 ryegrass. This species systemically colonises the aerial tissues of this host 21 where its growth is tightly regulated thereby maintaining a mutualistic symbiotic 42 proteins are either not required for the interaction at the observed life stages or 43 that there is redundancy between effectors expressed by E. festucae. 44 45 53 Cladosporium fulvum [2-4], as well as Pit2 and Rsp3 from the corn smut 54 pathogen Ustilago maydis [5, 6]. More specifically, Avr4 binds to chitin 55 molecules present in the cell wall of invading hyphae to prevent hydrolysis by 56 host chitinases [2, 7], while Ecp6 sequesters chitin oligosaccharides released 57 from the cell wall of invading hyphae to prevent detection by host chitin immune 58 receptors [4, 8]. Rsp3 binds to the cell wall of invading hyphae to protect them 59 against two antimicrobial mannose-binding host proteins [6], while both Pit2 60 and Avr2 inhibit host cysteine proteases to prevent degradation of fungal 61 proteins [3, 9-11]. A well-characterized example of an intracellular fungal 62 effector protein is Cmu1 from U. maydis, which functions as a chorismate 63 mutase to redirect the metabolism of chorismate away from the production of 64 the defense signaling hormone salicylic acid [12]. 4 65 Like plant-pathogenic fungi, plant-beneficial fungi must also deploy 66 effector proteins to promote host colonization [13, 14]. However, to date only a 67 small number of effectors from this group of fungi have been identified and 68 functionally characterized. Furthermore, of those that have been functionally 69 characterized all are from mycorrhizal fungi. One such example is MiSSP7 from 70 Laccaria bicolor, an ectomycorrhizal fungus of poplar roots. In plants (including 71 poplar), JAZ proteins repress the expression of jasmonic acid (JA)-related 72 defense genes, with the degradation of these proteins leading to the activation 73 of JA-related defense genes [15]. During infection of poplar, MiSSP7 is 74 transported into the plant nucleus where it interacts with and stabilizes the JAZ 75 protein PtJAZ6 to prevent its degradation, and thus prevent the expression of 76 JA defence-related genes [16, 17]. A second example is SP7, which is 77 produced by the arbuscular mycorrhizal fungus, Glomus intraradices. SP7, 78 which like PtJAZ6 is also transported into the plant nucleus, influences defense 79 gene signaling by interacting with the pathogenicity-related transcription factor 80 ERF12 [18]. A third example is Fgb1 has been characterized from the 81 endophytic root-colonizing fungus, Piriformospora indica. Fgb1 is a β-glucan-82 binding lectin that modulates the fungal cell composition and prevents β-glucan-83 triggered immunity in plants, presumably through a similar mechanism to that 84 shown for as Ecp6 and other LysM domain-containing effectors from plant-85 pathogenic fungi [19]. 86 There is little amino acid sequence conservation between effector 87 proteins of plant-associated fungi, and mo...

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Section: Discussionmentioning

confidence: 99%

Analysis of Epichloë festucae small secreted proteins in the interaction with Lolium perenne

Scott

Hassing

Winter

et al. 2018

Preprint

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“…Most fungal RiPPs have therefore been characterized through a top-down approach, leading to the identification of the amatoxins [37], phallotoxins [37], virotoxins (all reviewed in [38]), and more recently the epichloëcyclins [39], the ustiloxins [40], and the phomopsins [41]. Increasing knowledge of the biosynthetic enzymes associated with fungal RiPPs has revealed that the ustiloxins and phomopsins are widespread in the dikarya subkingdom [41,42].…”

Section: Examples Of Bottom-up Ripp Discoverymentioning

confidence: 99%

Ribosomally synthesized and post-translationally modified peptide natural product discovery in the genomic era

Hetrick

Donk

2017

Current Opinion in Chemical Biology

132

113

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In the past 15 years, the cost of sequencing a genome has plummeted. Consequently, the number of sequenced bacterial genomes has exponentially increased, and methods for natural product discovery have evolved rapidly to take advantage of the wealth of genomic data. This review highlights applications of genome mining software to compare and organize large-scale data sets and methods for identifying unique biosynthetic pathways amongst the thousands of ribosomally synthesized and post-translationally modified peptide (RiPP) gene clusters. We also discuss a small number of the many RiPPs discovered in the years 2014–2016.

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“…After identification of the ust cluster, we found more than 94 homologous clusters in Aspergillus genome sequences . Very recently, gene clusters for two RiPPs, epichloëcyclin and asperipin‐2a, have been reported . Herein, we report complete characterization of the formation of the core peptide by three oxidation enzymes uniquely found in the gene clusters of the filamentous fungal RiPPs, and subsequent modifications specific for ustiloxin biosynthesis.…”

Section: Figurementioning

confidence: 99%

“…In its biosynthetic gene cluster, which consists of four genes, the UstY homologue was found to be the sole oxidation enzyme. To date, only three gene clusters for the ribosomal peptides RiPPs have been characterized . However, a set of biosynthetic genes encoding a precursor peptide and UstY homologue have been identified in many fungal genomes .…”

Section: Figurementioning

confidence: 99%

“…To date, only three gene clusters for the ribosomal peptides RiPPs have been characterized . However, a set of biosynthetic genes encoding a precursor peptide and UstY homologue have been identified in many fungal genomes . This circumstantial evidence suggests that the most intriguing macrocyclization of the core peptide is catalyzed by a UstY homologue.…”

Section: Figurementioning

confidence: 99%

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Unveiling the Biosynthetic Pathway of the Ribosomally Synthesized and Post‐translationally Modified Peptide Ustiloxin B in Filamentous Fungi

Minami

Igarashi

et al. 2016

Angewandte Chemie

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The biosynthetic machinery of the first fungal ribosomally synthesized and post‐translationally modified peptide (RiPP) ustiloxin B was elucidated through a series of gene inactivation and heterologous expression studies. The results confirmed an essential requirement for novel oxidases possessing the DUF3328 motif for macrocyclization, and highly unique side‐chain modifications by three oxidases (UstCF1F2) and a pyridoxal 5′‐phosphate (PLP)‐dependent enzyme (UstD). These findings provide new insight into the expression of the RiPP gene clusters found in various fungi.

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A novel family of cyclic oligopeptides derived from ribosomal peptide synthesis of an in planta-induced gene, gigA, in Epichloë endophytes of grasses

Cited by 54 publications

References 58 publications

Analysis of Epichloë festucae small secreted proteins in the interaction with Lolium perenne

Analysis of Epichloë festucae small secreted proteins in the interaction with Lolium perenne

Ribosomally synthesized and post-translationally modified peptide natural product discovery in the genomic era

Unveiling the Biosynthetic Pathway of the Ribosomally Synthesized and Post‐translationally Modified Peptide Ustiloxin B in Filamentous Fungi

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