Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification |
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Authors: | Zhu Jianmei Zhu Shanshan Guzzo Catherine M Ellis Nathan A Sung Ki Sa Choi Cheol Yong Matunis Michael J |
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Affiliation: | ‡Bloomberg School of Public Health, Department of Biochemistry and Molecular Biology, The Johns Hopkins University, Baltimore, Maryland 21205, the §Department of Medicine, University of Chicago, Chicago, Illinois 60637, and the ¶Department of Biological Science, Sungkyunkwan University, 300 Chunchundong, Suwon 440-746, Korea |
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Abstract: | Small ubiquitin-related modifiers (SUMOs) regulate diverse cellular processes through their covalent attachment to target proteins. Vertebrates express three SUMO paralogs: SUMO-1, SUMO-2, and SUMO-3 (SUMO-2 and SUMO-3 are approximately 96% identical and referred to as SUMO-2/3). SUMO-1 and SUMO-2/3 are conjugated, at least in part, to unique subsets of proteins and thus regulate distinct cellular pathways. However, how different proteins are selectively modified by SUMO-1 and SUMO-2/3 is unknown. We demonstrate that BLM, the RecQ DNA helicase mutated in Bloom syndrome, is preferentially modified by SUMO-2/3 both in vitro and in vivo. Our findings indicate that non-covalent interactions between SUMO and BLM are required for modification at non-consensus sites and that preferential SUMO-2/3 modification is determined by preferential SUMO-2/3 binding. We also present evidence that sumoylation of a C-terminal fragment of HIPK2 is dependent on SUMO binding, indicating that non-covalent interactions between SUMO and target proteins provide a general mechanism for SUMO substrate selection and possible paralog-selective modification. |
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