Biosynthesis of isonitrile lipopeptides by conserved nonribosomal peptide synthetase gene clusters in Actinobacteria

A putative lipopeptide biosynthetic gene cluster is conserved in many species of Actinobacteria, including Mycobacterium tuberculosis and M. marinum, but the specific function of the encoding proteins has been elusive. Using both in vivo heterologous reconstitution and in vitro biochemical analyses,...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 114; no. 27; pp. 7025 - 7030
Main Authors Harris, Nicholas C., Sato, Michio, Herman, Nicolaus A., Twigg, Frederick, Cai, Wenlong, Liu, Joyce, Zhu, Xuejun, Downey, Jordan, Khalaf, Ryan, Martin, Joelle, Koshino, Hiroyuki, Zhang, Wenjun
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 03.07.2017
Subjects
Actinobacteria
Actinobacteria - enzymology
Actinobacteria - genetics
Acylation
Amino groups
Bacteria
Biological Sciences
Biological Transport
Biosynthesis
Catalysis
Chromatography
Chromatography, Ion Exchange
Enzymes
Escherichia coli - enzymology
Escherichia coli - genetics
Fatty Acids - chemistry
Gene clusters
Gene Deletion
Homology
Iron
Lipopeptides
Lipopeptides - biosynthesis
Lysine - chemistry
Metal concentrations
Metals
Multigene Family
Mutation
Mycobacterium marinum
Mycobacterium marinum - enzymology
Mycobacterium marinum - genetics
Mycobacterium tuberculosis
Mycobacterium tuberculosis - enzymology
Mycobacterium tuberculosis - genetics
Oxidase
Peptide Synthases - genetics
Peptide Synthases - metabolism
Peptides
Protein Domains
Proteins
Ribosomes - chemistry
Thioesterase
Tuberculosis
mycobacteria
biosynthetic enzymes
metal transport
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Abstract A putative lipopeptide biosynthetic gene cluster is conserved in many species of Actinobacteria, including Mycobacterium tuberculosis and M. marinum, but the specific function of the encoding proteins has been elusive. Using both in vivo heterologous reconstitution and in vitro biochemical analyses, we have revealed that the five encoding biosynthetic enzymes are capable of synthesizing a family of isonitrile lipopeptides (INLPs) through a thio-template mechanism. The biosynthesis features the generation of isonitrile from a single precursor Gly promoted by a thioesterase and a nonheme iron(II)-dependent oxidase homolog and the acylation of both amino groups of Lys by the same isonitrile acyl chain facilitated by a single condensation domain of a nonribosomal peptide synthetase. In addition, the deletion of INLP biosynthetic genes in M. marinum has decreased the intracellular metal concentration, suggesting the role of this biosynthetic gene cluster in metal transport.
AbstractList Mycobacterium tuberculosis is the leading causative agent of tuberculosis, from which millions die annually. A putative lipopeptide biosynthetic gene cluster has been shown to be essential for the survival of this pathogen in hosts, and homologous gene clusters have also been found in all pathogenic mycobacteria and other species of Actinobacteria. We have identified the function of these gene clusters in making a family of isonitrile lipopeptides. The biosynthesis has several unique features, including an unprecedented mechanism for isonitrile synthesis. Our results further suggest that these biosynthetic gene clusters play a role in metal transport and thus have shed light on a metal transport system that is crucial for virulence of pathogenic mycobacteria. A putative lipopeptide biosynthetic gene cluster is conserved in many species of Actinobacteria, including Mycobacterium tuberculosis and M. marinum , but the specific function of the encoding proteins has been elusive. Using both in vivo heterologous reconstitution and in vitro biochemical analyses, we have revealed that the five encoding biosynthetic enzymes are capable of synthesizing a family of isonitrile lipopeptides (INLPs) through a thio-template mechanism. The biosynthesis features the generation of isonitrile from a single precursor Gly promoted by a thioesterase and a nonheme iron(II)-dependent oxidase homolog and the acylation of both amino groups of Lys by the same isonitrile acyl chain facilitated by a single condensation domain of a nonribosomal peptide synthetase. In addition, the deletion of INLP biosynthetic genes in M. marinum has decreased the intracellular metal concentration, suggesting the role of this biosynthetic gene cluster in metal transport.
A putative lipopeptide biosynthetic gene cluster is conserved in many species of Actinobacteria, including Mycobacterium tuberculosis and M. marinum, but the specific function of the encoding proteins has been elusive. Using both in vivo heterologous reconstitution and in vitro biochemical analyses, we have revealed that the five encoding biosynthetic enzymes are capable of synthesizing a family of isonitrile lipopeptides (INLPs) through a thio-template mechanism. The biosynthesis features the generation of isonitrile from a single precursor Gly promoted by a thioesterase and a nonheme iron(II)-dependent oxidase homolog and the acylation of both amino groups of Lys by the same isonitrile acyl chain facilitated by a single condensation domain of a nonribosomal peptide synthetase. In addition, the deletion of INLP biosynthetic genes in M. marinum has decreased the intracellular metal concentration, suggesting the role of this biosynthetic gene cluster in metal transport.
A putative lipopeptide biosynthetic gene cluster is conserved in many species of Actinobacteria, including and , but the specific function of the encoding proteins has been elusive. Using both in vivo heterologous reconstitution and in vitro biochemical analyses, we have revealed that the five encoding biosynthetic enzymes are capable of synthesizing a family of isonitrile lipopeptides (INLPs) through a thio-template mechanism. The biosynthesis features the generation of isonitrile from a single precursor Gly promoted by a thioesterase and a nonheme iron(II)-dependent oxidase homolog and the acylation of both amino groups of Lys by the same isonitrile acyl chain facilitated by a single condensation domain of a nonribosomal peptide synthetase. In addition, the deletion of INLP biosynthetic genes in has decreased the intracellular metal concentration, suggesting the role of this biosynthetic gene cluster in metal transport.
Significance Mycobacterium tuberculosis is the leading causative agent of tuberculosis, from which millions die annually. A putative lipopeptide biosynthetic gene cluster has been shown to be essential for the survival of this pathogen in hosts, and homologous gene clusters have also been found in all pathogenic mycobacteria and other species of Actinobacteria. We have identified the function of these gene clusters in making a family of isonitrile lipopeptides. The biosynthesis has several unique features, including an unprecedented mechanism for isonitrile synthesis. Our results further suggest that these biosynthetic gene clusters play a role in metal transport and thus have shed light on a metal transport system that is crucial for virulence of pathogenic mycobacteria. A putative lipopeptide biosynthetic gene cluster is conserved in many species of Actinobacteria, including Mycobacterium tuberculosis and M. marinum , but the specific function of the encoding proteins has been elusive. Using both in vivo heterologous reconstitution and in vitro biochemical analyses, we have revealed that the five encoding biosynthetic enzymes are capable of synthesizing a family of isonitrile lipopeptides (INLPs) through a thio-template mechanism. The biosynthesis features the generation of isonitrile from a single precursor Gly promoted by a thioesterase and a nonheme iron(II)-dependent oxidase homolog and the acylation of both amino groups of Lys by the same isonitrile acyl chain facilitated by a single condensation domain of a nonribosomal peptide synthetase. In addition, the deletion of INLP biosynthetic genes in M. marinum has decreased the intracellular metal concentration, suggesting the role of this biosynthetic gene cluster in metal transport.
Author Twigg, Frederick
Liu, Joyce
Khalaf, Ryan
Martin, Joelle
Downey, Jordan
Harris, Nicholas C.
Koshino, Hiroyuki
Cai, Wenlong
Herman, Nicolaus A.
Zhang, Wenjun
Sato, Michio
Zhu, Xuejun
Author_xml – sequence: 1
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  organization: Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720
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  surname: Sato
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  organization: Department of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 422-8526, Japan
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  surname: Herman
  fullname: Herman, Nicolaus A.
  organization: Department of Chemical and Biomolecular Engineering, University of California, Berkeley, CA 94720
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  organization: Department of Chemical and Biomolecular Engineering, University of California, Berkeley, CA 94720
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Edited by Jerrold Meinwald, Cornell University, Ithaca, NY, and approved May 26, 2017 (received for review March 27, 2017)
Author contributions: N.C.H. and W.Z. designed research; N.C.H., M.S., N.A.H., F.T., W.C., J.L., X.Z., J.D., R.K., J.M., and W.Z. performed research; N.C.H., M.S., N.A.H., H.K., and W.Z. analyzed data; and N.C.H. and W.Z. wrote the paper.
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SSID ssj0009580
Score 2.4943552
Snippet A putative lipopeptide biosynthetic gene cluster is conserved in many species of Actinobacteria, including Mycobacterium tuberculosis and M. marinum, but the...
A putative lipopeptide biosynthetic gene cluster is conserved in many species of Actinobacteria, including and , but the specific function of the encoding...
Significance Mycobacterium tuberculosis is the leading causative agent of tuberculosis, from which millions die annually. A putative lipopeptide biosynthetic...
Mycobacterium tuberculosis is the leading causative agent of tuberculosis, from which millions die annually. A putative lipopeptide biosynthetic gene cluster...
SourceID pubmedcentral
proquest
crossref
pubmed
jstor
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 7025
SubjectTerms Actinobacteria
Actinobacteria - enzymology
Actinobacteria - genetics
Acylation
Amino groups
Bacteria
Biological Sciences
Biological Transport
Biosynthesis
Catalysis
Chromatography
Chromatography, Ion Exchange
Enzymes
Escherichia coli - enzymology
Escherichia coli - genetics
Fatty Acids - chemistry
Gene clusters
Gene Deletion
Homology
Iron
Lipopeptides
Lipopeptides - biosynthesis
Lysine - chemistry
Metal concentrations
Metals
Multigene Family
Mutation
Mycobacterium marinum
Mycobacterium marinum - enzymology
Mycobacterium marinum - genetics
Mycobacterium tuberculosis
Mycobacterium tuberculosis - enzymology
Mycobacterium tuberculosis - genetics
Oxidase
Peptide Synthases - genetics
Peptide Synthases - metabolism
Peptides
Protein Domains
Proteins
Ribosomes - chemistry
Thioesterase
Tuberculosis
Title Biosynthesis of isonitrile lipopeptides by conserved nonribosomal peptide synthetase gene clusters in Actinobacteria
URI https://www.jstor.org/stable/26485341
https://www.ncbi.nlm.nih.gov/pubmed/28634299
https://www.proquest.com/docview/1946414992/abstract/
https://search.proquest.com/docview/1912198447
https://pubmed.ncbi.nlm.nih.gov/PMC5502637
Volume 114
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