SUMOylation of PCNA with SUMO1

Stable Identifier
Reaction [transition]
Homo sapiens
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PCNA is SUMOylated with SUMO1 at lysine-164, lysine-254, and other residues (Papouli et al. 2005, Pfander et al. 2005, Gali et al. 2012, Impens et al. 2014). SUMO1 is predominant in vivo. SUMOylation prevents double strand break formation and recombination if DNA replication stalls at lesions (Gali et al. 2012). This is comparable to the situation in Saccharomyces cerevisiae where sumoylated PCNA recruits the Srs2 helicase to prevent recombination during S phase (Pfander et al. 2005, Papouli et al. 2005). In the yeast PCNA homolog, SUMO at lysine-164 is located on the opposite face of PCNA from the face that interacts with DNA polymerase (Freudenthal et al. 2011).

Literature References
PubMed ID Title Journal Year
21167178 Crystal structure of SUMO-modified proliferating cell nuclear antigen

Freudenthal, BD, Brogie, JE, Gakhar, L, Kondratick, CM, Washington, MT

J. Mol. Biol. 2011
22457066 Role of SUMO modification of human PCNA at stalled replication fork

Gali, H, Juhasz, S, Morocz, M, Hajdu, I, Fatyol, K, Szukacsov, V, Burkovics, P, Haracska, L

Nucleic Acids Res. 2012
15989970 Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p

Papouli, E, Chen, S, Davies, AA, Huttner, D, Krejci, L, Sung, P, Ulrich, HD

Mol. Cell 2005
15931174 SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase

Pfander, B, Moldovan, GL, Sacher, M, Hoege, C, Jentsch, S

Nature 2005
25114211 Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli

Impens, F, Radoshevich, L, Cossart, P, Ribet, D

Proc. Natl. Acad. Sci. U.S.A. 2014
Event Information
Go Biological Process
Catalyst Activity

SUMO transferase activity of SUMO1:C93-UBE2I [cytoplasm]

Orthologous Events
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