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

By M. Tatham, E. Jaffray, O. A. Vaughan, J. Desterro, C. Botting, J. Naismith, Ronald T. Hay. Journal of Biological Chemistry, 2001

879 citations recorded by the source corpus.

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 ψKXE, 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 detectedin 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.

Subfields: Molecular Biology, Parasitology

View Paper: https://www.semanticscholar.org/paper/67900cced0388904b60ea7e6900b2157d90cef9c

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In Molecular Biology

1. Toby J. Gibson
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Citations in the corpus

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