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Yeats, T.H., Department of Plant Biology, Cornell University, Ithaca, NY, United States
Martin, L.B.B., Department of Plant Biology, Cornell University, Ithaca, NY, United States
Viart, H.M.-F., Center for Nanomedicine and Theranostics, Technical University of Denmark, Lyngby, Denmark, Department of Chemistry, Technical University of Denmark, Lyngby, Denmark
Isaacson, T., Department of Plant Biology, Cornell University, Ithaca, NY, United States, Department of Fruit Sciences, Newe Ya'ar Research Center, Agricultural Research Organization, Ramat Yishay, Israel
He, Y., Department of Plant Biology, Cornell University, Ithaca, NY, United States
Zhao, L., Plant Biotechnology Research Center, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, China
Matas, A.J., Department of Plant Biology, Cornell University, Ithaca, NY, United States
Buda, G.J., Department of Plant Biology, Cornell University, Ithaca, NY, United States
Domozych, D.S., Department of Biology, Skidmore College, Saratoga Springs, NY, United States, Skidmore Microscopy Imaging Center, Skidmore College, Saratoga Springs, NY, United States
Clausen, M.H., Center for Nanomedicine and Theranostics, Technical University of Denmark, Lyngby, Denmark, Department of Chemistry, Technical University of Denmark, Lyngby, Denmark
Rose, J.K.C., Department of Plant Biology, Cornell University, Ithaca, NY, United States
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. © 2012 Nature America, Inc. All rights reserved.
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The identification of cutin synthase: Formation of the plant polyester cutin
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Yeats, T.H., Department of Plant Biology, Cornell University, Ithaca, NY, United States
Martin, L.B.B., Department of Plant Biology, Cornell University, Ithaca, NY, United States
Viart, H.M.-F., Center for Nanomedicine and Theranostics, Technical University of Denmark, Lyngby, Denmark, Department of Chemistry, Technical University of Denmark, Lyngby, Denmark
Isaacson, T., Department of Plant Biology, Cornell University, Ithaca, NY, United States, Department of Fruit Sciences, Newe Ya'ar Research Center, Agricultural Research Organization, Ramat Yishay, Israel
He, Y., Department of Plant Biology, Cornell University, Ithaca, NY, United States
Zhao, L., Plant Biotechnology Research Center, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, China
Matas, A.J., Department of Plant Biology, Cornell University, Ithaca, NY, United States
Buda, G.J., Department of Plant Biology, Cornell University, Ithaca, NY, United States
Domozych, D.S., Department of Biology, Skidmore College, Saratoga Springs, NY, United States, Skidmore Microscopy Imaging Center, Skidmore College, Saratoga Springs, NY, United States
Clausen, M.H., Center for Nanomedicine and Theranostics, Technical University of Denmark, Lyngby, Denmark, Department of Chemistry, Technical University of Denmark, Lyngby, Denmark
Rose, J.K.C., Department of Plant Biology, Cornell University, Ithaca, NY, United States
The identification of cutin synthase: Formation of the plant polyester cutin
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. © 2012 Nature America, Inc. All rights reserved.
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