Generation of SUMO-1 modified proteins in E. coli: towards understanding the biochemistry/structural biology of the SUMO-1 pathway.

Here, we developed a binary vector system that introduces a synthetic SUMO-1 conjugation pathway into Escherichia coli and demonstrated that large amounts of sumoylated Ran GTPase activating protein 1 C-terminal region (RanGAP1-C2), Ran binding protein 2 internal repeat domain, p53 and promyelocytic leukemia were efficiently produced. The sumoylated recombinant RanGAP1-C2 ...
appeared to retain the in vivo properties, since it was specifically sumoylated at lysine 517 as expected from in vivo studies. Our findings indicate the establishment of a biosynthetic route for producing large amounts of sumoylated recombinant proteins that will open up new avenues for studying the biochemical and structural aspects of the SUMO-1 modification pathway.
Mesh Terms:
Animals, Binding Sites, Cloning, Molecular, Escherichia coli, GTPase-Activating Proteins, Genetic Vectors, Mice, Protein Processing, Post-Translational, Recombinant Proteins, SUMO-1 Protein, Ubiquitin-Activating Enzymes
FEBS Lett.
Date: Apr. 23, 2004
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