A Unique Tryptophan C‐Prenyltransferase from the Kawaguchipeptin Biosynthetic Pathway

Anirudra Parajuli; Daniel H. Kwak; Luca Dalponte; Niina Leikoski; Tomas Galica; Ugochukwu Umeobika; Laurent Trembleau; Andrew Bent; Kaarina Sivonen; Matti Wahlsten; Hao Wang; Ermano Rizzi; Gianluca De Bellis; James Naismith; Marcel Jaspars; Xinyu Liu; Wael Houssen; David Peter Fewer

doi:10.1002/anie.201509920

A Unique Tryptophan C‐Prenyltransferase from the Kawaguchipeptin Biosynthetic Pathway

Anirudra Parajuli, Daniel H. Kwak, Luca Dalponte, Niina Leikoski, Tomas Galica, Ugochukwu Umeobika, Laurent Trembleau, Andrew Bent, Kaarina Sivonen, Matti Wahlsten, Hao Wang, Ermano Rizzi, Gianluca De Bellis, James Naismith, Marcel Jaspars, Xinyu Liu^* (Corresponding Author), Wael Houssen^* (Corresponding Author), David Peter Fewer^* (Corresponding Author)

^*Corresponding author for this work

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Abstract

Cyanobactins are a rapidly growing family of linear and cyclic peptides produced by cyanobacteria. Kawaguchipeptins A and B, two macrocyclic undecapeptides reported earlier from Microcystis aeruginosa NIES-88, are shown to be products of the cyanobactin biosynthetic pathway. The 9 kb kawaguchipeptin (kgp) gene cluster was identified in a 5.26 Mb draft genome of Microcystis aeruginosa NIES-88. We verified that this gene cluster is responsible for the production of the kawaguchipeptins through heterologous expression of the kgp gene cluster in Escherichia coli. The KgpF prenyltransferase was overexpressed and was shown to prenylate C-3 of Trp residues in both linear and cyclic peptides in vitro. Our findings serve to further enhance the structural diversity of cyanobactins to include tryptophan-prenylated cyclic peptides.

Original language	English
Pages (from-to)	3596-3599
Number of pages	4
Journal	Angewandte Chemie International Edition
Volume	55
Issue number	11
Early online date	5 Feb 2016
DOIs	https://doi.org/10.1002/anie.201509920
Publication status	Published - 7 Mar 2016

Bibliographical note

Acknowledgements

This work was supported by funding of the Academy of Finland (259505), Helsinki University Research grant (490085) and ESCMID grant (4720572) to D.P.F., University of Pittsburgh Central Research Development Fund to X.L., Technology Strategy Board grant (131181) to W.H., M.J. and J.H.N. National Programme of Sustainability I of the Ministry of Education of the Czech Republic I grant (LO1416) to T.G.

Keywords

biosynthesis
cyanobactins
peptides
prenylation
prenyltransferases

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Accepted Manuscript
This is the peer reviewed version of the following articleParajuli, A, Kwak, DH, Dalponte, L, Leikoski, N, Galica, T, Umeobika, U, Trembleau, L, Bent, A, Sivonen, K, Wahlsten, M, Wang, H, Rizzi, E, De Bellis, G, Naismith, J, Jaspars, M, Liu, X, Houssen, W & Fewer, DP 2016, 'A Unique Tryptophan C-Prenyltransferase from the Kawaguchipeptin Biosynthetic Pathway' Angewandte Chemie, vol 128, no. 11, pp. 3660–3663., which has been published in final form at doi: 10.1002/ange.201509920. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
Accepted author manuscript, 982 KBLicence: Unspecified

Wael E Houssen
Person: Academic
Marcel Jaspars
- Coastal Communities
- Engineering, National Decommissioning Centre
- School of Natural & Computing Sciences, Chemistry - Chair in Chemistry
Person: Academic
Laurent Trembleau
- School of Natural & Computing Sciences, Chemistry - Senior Lecturer
Person: Academic

Cite this

Parajuli, A., Kwak, D. H., Dalponte, L., Leikoski, N., Galica, T., Umeobika, U., Trembleau, L., Bent, A., Sivonen, K., Wahlsten, M., Wang, H., Rizzi, E., De Bellis, G., Naismith, J., Jaspars, M., Liu, X., Houssen, W., & Fewer, D. P. (2016). A Unique Tryptophan C‐Prenyltransferase from the Kawaguchipeptin Biosynthetic Pathway. Angewandte Chemie International Edition, 55(11), 3596-3599. https://doi.org/10.1002/anie.201509920

Parajuli, A, Kwak, DH, Dalponte, L, Leikoski, N, Galica, T, Umeobika, U, Trembleau, L, Bent, A, Sivonen, K, Wahlsten, M, Wang, H, Rizzi, E, De Bellis, G, Naismith, J, Jaspars, M, Liu, X, Houssen, W & Fewer, DP 2016, 'A Unique Tryptophan C‐Prenyltransferase from the Kawaguchipeptin Biosynthetic Pathway', Angewandte Chemie International Edition, vol. 55, no. 11, pp. 3596-3599. https://doi.org/10.1002/anie.201509920

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abstract = "Cyanobactins are a rapidly growing family of linear and cyclic peptides produced by cyanobacteria. Kawaguchipeptins A and B, two macrocyclic undecapeptides reported earlier from Microcystis aeruginosa NIES-88, are shown to be products of the cyanobactin biosynthetic pathway. The 9 kb kawaguchipeptin (kgp) gene cluster was identified in a 5.26 Mb draft genome of Microcystis aeruginosa NIES-88. We verified that this gene cluster is responsible for the production of the kawaguchipeptins through heterologous expression of the kgp gene cluster in Escherichia coli. The KgpF prenyltransferase was overexpressed and was shown to prenylate C-3 of Trp residues in both linear and cyclic peptides in vitro. Our findings serve to further enhance the structural diversity of cyanobactins to include tryptophan-prenylated cyclic peptides.",

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N1 - Acknowledgements This work was supported by funding of the Academy of Finland (259505), Helsinki University Research grant (490085) and ESCMID grant (4720572) to D.P.F., University of Pittsburgh Central Research Development Fund to X.L., Technology Strategy Board grant (131181) to W.H., M.J. and J.H.N. National Programme of Sustainability I of the Ministry of Education of the Czech Republic I grant (LO1416) to T.G.

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AB - Cyanobactins are a rapidly growing family of linear and cyclic peptides produced by cyanobacteria. Kawaguchipeptins A and B, two macrocyclic undecapeptides reported earlier from Microcystis aeruginosa NIES-88, are shown to be products of the cyanobactin biosynthetic pathway. The 9 kb kawaguchipeptin (kgp) gene cluster was identified in a 5.26 Mb draft genome of Microcystis aeruginosa NIES-88. We verified that this gene cluster is responsible for the production of the kawaguchipeptins through heterologous expression of the kgp gene cluster in Escherichia coli. The KgpF prenyltransferase was overexpressed and was shown to prenylate C-3 of Trp residues in both linear and cyclic peptides in vitro. Our findings serve to further enhance the structural diversity of cyanobactins to include tryptophan-prenylated cyclic peptides.

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KW - cyanobactins

KW - peptides

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A Unique Tryptophan C‐Prenyltransferase from the Kawaguchipeptin Biosynthetic Pathway

Abstract

Bibliographical note

Keywords

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Wael E Houssen

Marcel Jaspars

Laurent Trembleau

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