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Drosophila melanogaster nonribosomal peptide synthetase Ebony encodes an atypical condensation domain.

Izoré T, Tailhades J, Hansen MH, Kaczmarski JA, Jackson CJ, Cryle MJ
Proc Natl Acad Sci U S A 116 2913-2918 (2019)
Related entries: 6dym, 6dyn, 6dyo, 6dyr

Cited: 12 times
EuropePMC logo PMID: 30705105

Abstract

The protein Ebony from Drosophila melanogaster plays a central role in the regulation of histamine and dopamine in various tissues through condensation of these amines with β-alanine. Ebony is a rare example of a nonribosomal peptide synthetase (NRPS) from a higher eukaryote and contains a C-terminal sequence that does not correspond to any previously characterized NRPS domain. We have structurally characterized this C-terminal domain and have discovered that it adopts the aryl-alkylamine-N-acetyl transferase (AANAT) fold, which is unprecedented in NRPS biology. Through analysis of ligand-bound structures, activity assays, and binding measurements, we have determined how this atypical condensation domain is able to provide selectivity for both the carrier protein-bound amino acid and the amine substrates, a situation that remains unclear for standard condensation domains identified to date from NRPS assembly lines. These results demonstrate that the C terminus of Ebony encodes a eukaryotic example of an alternative type of NRPS condensation domain; they also illustrate how the catalytic components of such assembly lines are significantly more diverse than a minimal set of conserved functional domains.

Articles - 6dys mentioned but not cited (1)

  1. Drosophila melanogaster nonribosomal peptide synthetase Ebony encodes an atypical condensation domain. Izoré T, Tailhades J, Hansen MH, Kaczmarski JA, Jackson CJ, Cryle MJ. Proc Natl Acad Sci U S A 116 2913-2918 (2019)


Reviews citing this publication (4)

  1. Mining genomes to illuminate the specialized chemistry of life. Medema MH, de Rond T, Moore BS. Nat Rev Genet 22 553-571 (2021)
  2. The biosynthetic diversity of the animal world. Torres JP, Schmidt EW. J Biol Chem 294 17684-17692 (2019)
  3. Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases. Patel KD, MacDonald MR, Ahmed SF, Singh J, Gulick AM. Nat Prod Rep 40 1550-1582 (2023)
  4. Nonribosomal Peptide Synthetases in Animals. Suring W, Hoogduin D, Le Ngoc G, Brouwer A, van Straalen NM, Roelofs D. Genes (Basel) 14 1741 (2023)

Articles citing this publication (7)

  1. Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity. Izoré T, Candace Ho YT, Kaczmarski JA, Gavriilidou A, Chow KH, Steer DL, Goode RJA, Schittenhelm RB, Tailhades J, Tosin M, Challis GL, Krenske EH, Ziemert N, Jackson CJ, Cryle MJ. Nat Commun 12 2511 (2021)
  2. A proof-reading mechanism for non-proteinogenic amino acid incorporation into glycopeptide antibiotics. Kaniusaite M, Tailhades J, Marschall EA, Goode RJA, Schittenhelm RB, Cryle MJ. Chem Sci 10 9466-9482 (2019)
  3. A male-derived nonribosomal peptide pheromone controls female schistosome development. Chen R, Wang J, Gradinaru I, Vu HS, Geboers S, Naidoo J, Ready JM, Williams NS, DeBerardinis RJ, Ross EM, Collins JJ. Cell 185 1506-1520.e17 (2022)
  4. Drosophila melanogaster Uncoupling Protein-4A (UCP4A) Catalyzes a Unidirectional Transport of Aspartate. Lunetti P, Gorgoglione R, Curcio R, Marra F, Pignataro A, Vozza A, Riley CL, Capobianco L, Palmieri L, Dolce V, Fiermonte G. Int J Mol Sci 23 1020 (2022)
  5. Gcn5-Related N-Acetyltransferases (GNATs) With a Catalytic Serine Residue Can Play Ping-Pong Too. Baumgartner JT, Habeeb Mohammad TS, Czub MP, Majorek KA, Arolli X, Variot C, Anonick M, Minor W, Ballicora MA, Becker DP, Kuhn ML. Front Mol Biosci 8 646046 (2021)
  6. Host Defense Peptide Piscidin and Yeast-Derived Glycolipid Exhibit Synergistic Antimicrobial Action through Concerted Interactions with Membranes. Liu F, Greenwood AI, Xiong Y, Miceli RT, Fu R, Anderson KW, McCallum SA, Mihailescu M, Gross R, Cotten ML. JACS Au 3 3345-3365 (2023)
  7. P450-mediated dehydrotyrosine formation during WS9326 biosynthesis proceeds via dehydrogenation of a specific acylated dipeptide substrate. Zhang S, Zhang L, Greule A, Tailhades J, Marschall E, Prasongpholchai P, Leng DJ, Zhang J, Zhu J, Kaczmarski JA, Schittenhelm RB, Einsle O, Jackson CJ, Alberti F, Bechthold A, Zhang Y, Tosin M, Si T, Cryle MJ. Acta Pharm Sin B 13 3561-3574 (2023)


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