PMID- 10187858
OWN - NLM
STAT- MEDLINE
DCOM- 19990503
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 15
DP  - 1999 Apr 9
TI  - Identification of the enzyme required for activation of the small ubiquitin-like 
      protein SUMO-1.
PG  - 10618-24
AB  - The ubiquitin-like protein SUMO-1 is conjugated to a variety of proteins
      including Ran GTPase-activating protein 1 (RanGAP1), IkappaBalpha, 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 IkappaBalpha. As SAE1/SAE2, Ubch9, SUMO-1, and IkappaBalpha are all
      homogeneous, recombinant proteins, it appears that SUMO-1 conjugation of
      IkappaBalpha in vitro does not require the equivalent of an E3 ubiquitin protein 
      ligase activity.
FAU - Desterro, J M
AU  - Desterro JM
AD  - School of Biomedical Science, University of St. Andrews, St. Andrews, Fife
      KY169ST Scotland.
FAU - Rodriguez, M S
AU  - Rodriguez MS
FAU - Kemp, G D
AU  - Kemp GD
FAU - Hay, R T
AU  - Hay RT
LA  - eng
SI  - GENBANK/AF110956
SI  - GENBANK/AF110957
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (I-kappa B Proteins)
RN  - 0 (NFKBIA protein, human)
RN  - 0 (RUB1 protein, S cerevisiae)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Repressor Proteins)
RN  - 0 (SUMO-1 Protein)
RN  - 0 (SUMO2 protein, human)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Small Ubiquitin-Related Modifier Proteins)
RN  - 0 (UBA2 protein, human)
RN  - 0 (Ubiquitins)
RN  - 139874-52-5 (NF-KappaB Inhibitor alpha)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
RN  - EC 6.- (Ligases)
RN  - EC 6.2.1.45 (SAE1 protein, human)
RN  - EC 6.2.1.45 (Ubiquitin-Activating Enzymes)
SB  - IM
MH  - Adenosine Triphosphate/metabolism
MH  - Amino Acid Sequence
MH  - Chromatography, Affinity
MH  - Cloning, Molecular
MH  - DNA-Binding Proteins/metabolism
MH  - Fungal Proteins/chemistry/metabolism
MH  - HeLa Cells
MH  - Humans
MH  - *I-kappa B Proteins
MH  - Ligases/genetics/*isolation & purification/metabolism
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - NF-KappaB Inhibitor alpha
MH  - Protein Conformation
MH  - Recombinant Proteins
MH  - Repressor Proteins/chemistry/metabolism
MH  - SUMO-1 Protein
MH  - *Saccharomyces cerevisiae Proteins
MH  - *Sequence Homology, Amino Acid
MH  - *Small Ubiquitin-Related Modifier Proteins
MH  - Ubiquitin-Activating Enzymes
MH  - Ubiquitin-Protein Ligases
MH  - Ubiquitins/*metabolism
EDAT- 1999/04/03 00:00
MHDA- 1999/04/03 00:01
CRDT- 1999/04/03 00:00
PHST- 1999/04/03 00:00 [pubmed]
PHST- 1999/04/03 00:01 [medline]
PHST- 1999/04/03 00:00 [entrez]
AID - 10.1074/jbc.274.15.10618 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 9;274(15):10618-24. doi: 10.1074/jbc.274.15.10618.