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J Biol Chem, Vol. 274, Issue 15, 10618-10624, April 9, 1999
From the School of Biomedical Science, University of St. Andrews,
St. Andrews, Fife KY169ST Scotland
The ubiquitin-like protein SUMO-1 is conjugated
to a variety of proteins including Ran GTPase-activating protein 1 (RanGAP1), I
Identification of the Enzyme Required for Activation of the Small
Ubiquitin-like Protein SUMO-1
B
, and PML. SUMO-1-modified proteins display altered
subcellular targeting and/or stability. We have purified the
SUMO-1-activating enzyme from human cells and shown that it contains
two subunits of 38 and 72 kDa. Isolation of cDNAs for each subunit
indicates that they are homologous to ubiquitin-activating enzymes and
to the Saccharomyces cerevisiae enzymes responsible for
conjugation of Smt3p and Rub-1p. In vitro, recombinant
SAE1/SAE2 (SUMO-1-activating enzyme) was capable of catalyzing the
ATP-dependent formation of a thioester linkage between
SUMO-1 and SAE2. The addition of the SUMO-1-conjugating enzyme Ubch9
resulted in efficient transfer of the thioester-linked SUMO-1 from SAE2
to Ubch9. In the presence of SAE1/SAE2, Ubch9, and ATP, SUMO-1 was
efficiently conjugated to the protein substrate IB. As SAE1/SAE2,
Ubch9, SUMO-1, and IB are all homogeneous, recombinant proteins,
it appears that SUMO-1 conjugation of IB in vitro
does not require the equivalent of an E3 ubiquitin protein ligase activity.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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