TY - JOUR
T1 - Polymeric Chains of SUMO-2 and SUMO-3 Are Conjugated to Protein Substrates by SAE1/SAE2 and Ubc9
AU - Tatham, Michael Howard
AU - Jaffray, Ellis
AU - Vaughan, Tony
AU - Desterro, Joana MP
AU - Botting, Catherine Helen
AU - Naismith, James Henderson
AU - Hay, Ronald Thomas
N1 - SUMO-2 /-3, unlike SUMO-1, contain the sequence KXE, the consensus SUMO modification site. It was postulated SUMO-2 /-3 could form Ubiquitin-like polymeric chains. The presence of these isopeptide bond linkages was proved by mass spectrometry. This publication showed SUMO-2 /-3 must play a different role in the cell to SUMO-1.
Funding: UK Medical Research Council
PY - 2001/9/21
Y1 - 2001/9/21
N2 - 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.
AB - 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.
KW - Ubiquitin-like proteins
KW - Nuclear-pore complex
KW - Kappa-B-alpha
KW - Covalent modification
KW - Sentrin family
KW - PML
KW - Activation
KW - RANGAP1
KW - p53
UR - http://www.scopus.com/inward/record.url?scp=0035929557&partnerID=8YFLogxK
UR - http://www.jbc.org/cgi/reprint/276/38/35368
U2 - 10.1074/jbc.M104214200
DO - 10.1074/jbc.M104214200
M3 - Article
SN - 0021-9258
VL - 276
SP - 35368
EP - 35374
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 38
ER -