Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9.
Conjugation of the small ubiquitin-like modifier SUMO-1/SMT3C/Sentrin-1 to proteins in vitro is dependent on a heterodimeric E1 (SAE1/SAE2) and an E2 (Ubc9). Although SUMO-2/SMT3A/Sentrin-3 and SUMO-3/SMT3B/Sentrin-2 share 50% sequence identity with SUMO-1, they are functionally distinct. Inspection of the SUMO-2 and SUMO-3 sequences indicates that they both contain the sequence ... psiKXE, which represents the consensus SUMO modification site. As a consequence SAE1/SAE2 and Ubc9 catalyze the formation of polymeric chains of SUMO-2 and SUMO-3 on protein substrates in vitro, and SUMO-2 chains are detected in vivo. The ability to form polymeric chains is not shared by SUMO-1, and although all SUMO species use the same conjugation machinery, modification by SUMO-1 and SUMO-2/-3 may have distinct functional consequences.
Mesh Terms:
Amino Acid Sequence, Base Sequence, Biopolymers, Cell Line, DNA Primers, Endonucleases, Fungal Proteins, Humans, Ligases, Lysine, Molecular Sequence Data, Nuclear Cap-Binding Protein Complex, Phosphoproteins, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Small Ubiquitin-Related Modifier Proteins, Substrate Specificity, Ubiquitin-Conjugating Enzymes, Ubiquitins
Amino Acid Sequence, Base Sequence, Biopolymers, Cell Line, DNA Primers, Endonucleases, Fungal Proteins, Humans, Ligases, Lysine, Molecular Sequence Data, Nuclear Cap-Binding Protein Complex, Phosphoproteins, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Small Ubiquitin-Related Modifier Proteins, Substrate Specificity, Ubiquitin-Conjugating Enzymes, Ubiquitins
J. Biol. Chem.
Date: Sep. 21, 2001
PubMed ID: 11451954
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