Plant Physiology Preview
Published on August 18, 2006; 10.1104/pp.106.085415
Received June 20, 2006
Accepted July 14, 2006
SUMO Conjugating and De-conjugating Enzymes from Arabidopsis
Thomas Colby , Anett Matthäi , Astrid Boeckelmann , and Hans-Peter Stuible *
Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linnè Weg 10, 50829 Cologne, Germany
* Corresponding author; email: stuible{at}mpiz-koeln.mpg.de.
Posttranslational protein modification by the small ubiquitin-like modifier (SUMO) is a highly dynamic and reversible process. To analyze the substrate specificity of SUMO-conjugating and de-conjugating enzymes from Arabidopsis, we reconstituted its SUMOylation cascade in vitro and tested the capacity of this system to conjugate the Arabidopsis SUMO isoforms AtSUMO1, 2 and 3 to the model substrate ScPCNA from yeast. This protein contains two in vivo SUMOylated lysine residues, namely K127 and K164. Under in vitro conditions, the Arabidopsis SUMOylation system specifically conjugates all tested SUMO isoforms to lysine 127 but not to lysine 164 of ScPCNA. The SUMO isoforms AtSUMO1 and AtSUMO2 but not AtSUMO3 were found to form polymeric-chains on ScPCNA due to a self-SUMOylation process. In a complementary approach we analyzed both the SUMO isopeptidase activity and the pre-SUMO processing capacity of the putative Arabidopsis SUMO proteases At1g60220, At1g10570 and At5g60190 using the known SUMO isopeptidases ScULP1, XopD and ESD4 (At4g15880) as reference enzymes. Interestingly, At5g60190 exhibits no SUMO protease activity but processes the pre-form of Arabidopsis Rub1. The other five enzymes represent SUMO isopeptidases that show different substrate preferences. All these enzymes cleave AtSUMO1 and AtSUMO2 conjugates of ScPCNA, whereas only the putative bacterial virulence factor XopD is able to release AtSUMO3. In addition, all five enzymes cleave pre-AtSUMO1 and pre-AtSUMO2 peptides, but none of the proteins efficiently produce mature AtSUMO3 or AtSUMO5 molecules from their precursors.
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