Structural analysis of poly-SUMO chain recognition by the RNF4-SIMs domain

Camy C H Kung, Mandar T. Naik, Szu Huan Wang, Hsiu Ming Shih, Che Chang Chang, Li Ying Lin, Chia Lin Chen, Che Ma, Chi Fon Chang, Tai Huang Huang

研究成果: 雜誌貢獻文章

14 引文 斯高帕斯(Scopus)

摘要

The E3 ubiquitin ligase RNF4 (RING finger protein 4) contains four tandem SIM [SUMO (small ubiquitin-like modifier)-interaction motif] repeats for selective interaction with poly-SUMO-modified proteins, which it targets for degradation. We employed a multi-faceted approach to characterize the structure of the RNF4-SIMs domain and the tetra-SUMO2 chain to elucidate the interaction between them. In solution, the SIM domainwas intrinsically disordered and the linkers of the tetra-SUMO2 were highly flexible. Individual SIMs of the RNF4-SIMs domains bind to SUMO2 in the groove between the β2-strand and the α1-helix parallel to the β2-strand. SIM2 and SIM3 bound to SUMO with a high affinity and together constituted the recognition module necessary for SUMO binding. SIM4 alone bound to SUMO with low affinity; however, its contribution to tetra-SUMO2 binding avidity is comparable with that of SIM3 when in the RNF4-SIMs domain. The SAXS data of the tetra-SUMO2-RNF4-SIMs domain complex indicate that it exists as an ordered structure. The HADDOCK model showed that the tandem RNF4-SIMs domain bound antiparallel to the tetra-SUMO2 chain orientation and wrapped around the SUMO protamers in a superhelical turn without imposing steric hindrance on either molecule.
原文英語
頁(從 - 到)53-65
頁數13
期刊Biochemical Journal
462
發行號1
DOIs
出版狀態已發佈 - 七月 15 2014

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

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    Kung, C. C. H., Naik, M. T., Wang, S. H., Shih, H. M., Chang, C. C., Lin, L. Y., Chen, C. L., Ma, C., Chang, C. F., & Huang, T. H. (2014). Structural analysis of poly-SUMO chain recognition by the RNF4-SIMs domain. Biochemical Journal, 462(1), 53-65. https://doi.org/10.1042/BJ20140521