Journal of Biological Chemistry
Volume 276, Issue 36, 7 September 2001, Pages 33547-33553
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PROTEIN SYNTHESIS POST-TRANSLATION MODIFICATION AND DEGRADATION
Barley Lipid Transfer Protein, LTP1, Contains a New Type of Lipid-like Post-translational Modification*

https://doi.org/10.1074/jbc.M104841200Get rights and content
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In plants a group of proteins termed nonspecific lipid transfer proteins are found. These proteins bind and catalyze transfer of lipids in vitro, but their in vivofunction is unknown. They have been suggested to be involved in different aspects of plant physiology and cell biology, including the formation of cutin and involvement in stress and pathogen responses, but there is yet no direct demonstration of an in vivofunction. We have found and characterized a novel post-translational modification of the barley nonspecific lipid transfer protein, LTP1. The protein-modification bond is of a new type in which an aspartic acid in LTP1 is bound to the modification through what most likely is an ester bond. The chemical structure of the modification has been characterized by means of two-dimensional homo- and heteronuclear nuclear magnetic resonance spectroscopy as well as mass spectrometry and is found to be lipid-like in nature. The modification does not resemble any standard lipid post-translational modification but is similar to a compound with known antimicrobial activity.

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Published, JBC Papers in Press, June 30, 2001, DOI 10.1074/jbc.M104841200

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Supported by a scholarship from the University of Copenhagen.