Polymeric Chains of SUMO-2 and SUMO-3 Are Conjugated to Protein Substrates by SAE1/SAE2 and Ubc9

Michael Howard Tatham, Ellis Jaffray, Tony Vaughan, Joana MP Desterro, Catherine Helen Botting, James Henderson Naismith, Ronald Thomas Hay

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602 Citations (Scopus)


Conjugation of the small ubiquitin-like modifier SUMO-1/SMT3C/Sentrin-1 to proteins in vitro is dependent on a heterodimeric El (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 psi KXE, 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.

Original languageEnglish
Pages (from-to)35368-35374
Number of pages7
JournalJournal of Biological Chemistry
Issue number38
Early online date12 Jul 2001
Publication statusPublished - 21 Sept 2001


  • Ubiquitin-like proteins
  • Nuclear-pore complex
  • Kappa-B-alpha
  • Covalent modification
  • Sentrin family
  • PML
  • Activation
  • p53


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