Article abstract
Nature Chemical Biology 4, 557 - 563 (2008)
Published online: 27 July 2008 | doi:10.1038/nchembio.104
-Lactone probes identify a papain-like peptide ligase in Arabidopsis thaliana
Zheming Wang1,2,6, Christian Gu1,6, Tom Colby3, Takayuki Shindo1, Rengarajan Balamurugan4,5, Herbert Waldmann4, Markus Kaiser2 & Renier A L van der Hoorn1,2
Abstract
New activity-based probes are essential for expanding studies on the hundreds of serine and cysteine proteases encoded by the genome of Arabidopsis thaliana. To monitor protease activities in plant extracts, we generated biotinylated peptides containing a 
-lactone reactive group. These probes cause strong labeling in leaf proteomes. Unexpectedly, labeling was detected at the N terminus of PsbP, nonproteolytic protein of photosystem II. Inhibitor studies and reverse genetics led to the discovery that this unusual modification is mediated by a single plant-specific, papain-like protease called RD21. In cellular extracts, RD21 accepts both -lactone probes and peptides as donor molecules and ligates them, probably through a thioester intermediate, to unmodified N termini of acceptor proteins.
- Plant Chemetics Lab, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, 50829 Cologne, Germany.
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Chemical Genomics Centre of the Max Planck Society, Otto-Hahn-Stra
e 11, 44227 Dortmund, Germany. - Proteomics Service Centre, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, 50829 Cologne, Germany.
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Max Planck Institute for Molecular Physiology, Otto-Hahn-Strae 11, 44227 Dortmund, Germany.
- School of Chemistry, University of Hyderabad, Gachi Bowli, Hyderabad 500 046, India.
- These authors contributed equally to this work.
Correspondence to: Renier A L van der Hoorn1,2 e-mail: hoorn@mpiz-koeln.mpg.de
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