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  The nitrilase PtNIT1 catabolizes herbivoreinduced nitriles in Populus trichocarpa

Günther, J., Irmisch, S., Lackus, N., Reichelt, M., Gershenzon, J., & Köllner, T. G. (2018). The nitrilase PtNIT1 catabolizes herbivoreinduced nitriles in Populus trichocarpa. BMC Plant Biology, 18: 251. doi:10.1186/s12870-018-1478-z.

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http://dx.doi.org/10.1186/s12870-018-1478-z (Publisher version)
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 Creators:
Günther, Jan1, 2, Author              
Irmisch, Sandra1, Author              
Lackus, Nathalie1, 2, Author              
Reichelt, Michael1, Author              
Gershenzon, Jonathan1, Author              
Köllner, Tobias G.1, Author              
Affiliations:
1Department of Biochemistry, Prof. J. Gershenzon, MPI for Chemical Ecology, Max Planck Society, ou_421893              
2IMPRS on Ecological Interactions, MPI for Chemical Ecology, Max Planck Society, Jena, DE, ou_421900              

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 Abstract: Background: Nitrilases are nitrile-converting enzymes commonly found within the plant kingdom that play diverse roles in nitrile detoxification, nitrogen recycling, and phytohormone biosynthesis. Although nitrilases are present in all higher plants, little is known about their function in trees. Upon herbivory, poplars produce considerable amounts of toxic nitriles such as benzyl cyanide, 2-methylbutyronitrile, and 3-methylbutyronitrile. In addition, as byproduct of the ethylene biosynthetic pathway upregulated in many plant species after herbivory, toxic β-cyanoalanine may accumulate in damaged poplar leaves. In this work, we studied the nitrilase gene family in Populus trichocarpa and investigated the potential role of the nitrilase PtNIT1 in the catabolism of herbivore-induced nitriles. Results: A BLAST analysis revealed three putative nitrilase genes (PtNIT1, PtNIT2, PtNIT3) in the genome of P. trichocarpa. While PtNIT1 was expressed in poplar leaves and showed increased transcript accumulation after leaf herbivory, PtNIT2 and PtNIT3 appeared not to be expressed in undamaged or herbivore-damaged leaves. Recombinant PtNIT1 produced in Escherichia coli accepted biogenic nitriles such as β-cyanoalanine, benzyl cyanide, and indole-3-acetonitrile as substrates in vitro and converted them into the corresponding acids. In addition to this nitrilase activity, PtNIT1 showed nitrile hydratase activity towards β-cyanoalanine, resulting in the formation of the amino acid asparagine. The kinetic parameters of PtNIT1 suggest that the enzyme utilizes β-cyanoalanine and benzyl cyanide as substrates in vivo. Indeed, β-cyanoalanine and benzyl cyanide were found to accumulate in herbivore-damaged poplar leaves. The upregulation of ethylene biosynthesis genes after leaf herbivory indicates that herbivore-induced β-cyanoalanine accumulation is likely caused by ethylene formation.

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 Dates: 2018-10-102018-10-11
 Publication Status: Published online
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 Rev. Type: -
 Identifiers: Other: GER531
DOI: 10.1186/s12870-018-1478-z
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Title: BMC Plant Biology
Source Genre: Journal
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Publ. Info: BioMed Central
Pages: - Volume / Issue: 18 Sequence Number: 251 Start / End Page: - Identifier: ISSN: 1471-2229
CoNE: https://pure.mpg.de/cone/journals/resource/111032787578000