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The identification of cutin synthase: formation of the plant polyester cutin

Nature Chemical Biology volume 8, pages 609–611 (2012)Cite this article

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Abstract

A hydrophobic cuticle consisting of waxes and the polyester cutin covers the aerial epidermis of all land plants, providing essential protection from desiccation and other stresses. We have determined the enzymatic basis of cutin polymerization through characterization of a tomato extracellular acyltransferase, CD1, and its substrate, 2-mono(10,16-dihydroxyhexadecanoyl)glycerol. CD1 has in vitro polyester synthesis activity and is required for cutin accumulation in vivo, indicating that it is a cutin synthase.

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Figure 1: CD1 is a GDSL family protein that localizes to the nascent cuticle.
Figure 2: The identification of 2-MHG in the soluble surface lipids of cd1 fruit.
Figure 3: Acyltransferase activity of CD1.

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Acknowledgements

We thank G. Lomonossoff (John Innes Centre) and Plant Bioscience Limited for the pEAQ vector, M. Toso for help with transmission electron microscopy, S. Zhang and B. Sherwood for assistance with MALDI-TOF MS and M. Pollard and K. Niklas for critical discussion. This work was supported by grants from the US National Science Foundation (Plant Genome Program; DBI-0606595), the United States–Israel Binational Agricultural Research and Development Fund (IS-4234-09); the US Department of Agriculture Cooperative State Research, Education and Extension Service (2011-04197); and the Danish Council for Strategic Research (10-093465). T.H.Y. was supported in part by a US National Institutes of Health Chemistry-Biology Interface Training Grant (T32 GM008500).

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Author notes

  1. Tal Isaacson

    Present address: Present address: Department of Fruit Sciences, Newe Ya'ar Research Center, Agricultural Research Organization, Ramat Yishay, Israel.,

  2. Trevor H Yeats and Laetitia B B Martin: These authors contributed equally to this work.

Authors and Affiliations

  1. Department of Plant Biology, Cornell University, Ithaca, New York, USA

    Trevor H Yeats, Laetitia B B Martin, Tal Isaacson, Yonghua He, Antonio J Matas, Gregory J Buda & Jocelyn K C Rose

  2. Center for Nanomedicine and Theranostics, Technical University of Denmark, Lyngby, Denmark

    Hélène M-F Viart & Mads H Clausen

  3. Department of Chemistry, Technical University of Denmark, Lyngby, Denmark

    Hélène M-F Viart & Mads H Clausen

  4. Plant Biotechnology Research Center, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, China

    Lingxia Zhao

  5. Department of Biology, Skidmore College, Saratoga Springs, New York, USA

    David S Domozych

  6. Skidmore Microscopy Imaging Center, Skidmore College, Saratoga Springs, New York, USA

    David S Domozych

Authors
  1. Trevor H Yeats
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Contributions

T.H.Y. purified recombinant protein and performed chemical analysis of soluble surface lipids and acyltransferase assays. L.B.B.M. performed gene and protein expression experiments and cutin analysis. H.M.-F.V. and M.H.C. synthesized 2-MHG. T.I. identified and performed initial characterization and rough mapping of the mutant. Y.H. and L.Z. performed fine genetic mapping experiments and constructed the transgenic complementation vector. A.J.M. performed the tissue-specific gene expression experiments. G.J.B. conducted light microscopy experiments. L.B.B.M. and D.S.D. performed immunolocalization experiments. T.H.Y., L.B.B.M. and J.K.C.R. designed the study, analyzed the data and wrote the paper.

Corresponding author

Correspondence to Jocelyn K C Rose.

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The authors declare no competing financial interests.

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Yeats, T., Martin, L., Viart, HF. et al. The identification of cutin synthase: formation of the plant polyester cutin. Nat Chem Biol 8, 609–611 (2012). https://doi.org/10.1038/nchembio.960

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