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In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
Published on: November 2, 2017
The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during
Lin Nan Shen1, Changjiang Dong, Huanting Liu
1Centre for Biomolecular Sciences, University of St. Andrews, St. Andrews, Scotland KY16 9ST, UK.
The Biochemical Journal
|March 24, 2006
Summary
The SUMO-specific protease SENP1 shows substrate selectivity, primarily due to electrostatic interactions between the protease and SUMO C-terminal peptides, explaining its processing efficiency differences.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- SENP1 (sentrin-specific protease 1) is a SUMO (small ubiquitin-like modifier)-specific protease.
- SENP1 processes SUMO proteins into mature forms and removes SUMO from substrates.
- Previous studies showed SENP1 processes SUMO-1 more efficiently than SUMO-2 but deconjugates both similarly.
Purpose of the Study:
- To elucidate the structural basis for SENP1's substrate specificity in SUMO processing.
- To understand the molecular interactions governing SENP1's differential activity towards SUMO paralogues.
Main Methods:
- Determined crystal structures of SENP1 alone and in a transition-state complex with SUMO-2.
- Analyzed the interface between SENP1 and SUMO-2.
- Performed electrostatic analysis of SENP1.
Main Results:
- The interface between SENP1 and SUMO-2 shows poor complementarity.
- Recognition is largely mediated by the SUMO-2 C-terminus interacting with the SENP1 cleft.
- Electrostatic complementarity in a specific region of SENP1 dictates selectivity for different SUMO paralogues.
Conclusions:
- SENP1's substrate selectivity is primarily driven by electrostatic interactions with SUMO C-terminal peptides.
- This electrostatic complementarity explains the observed differences in processing efficiency between SUMO paralogues.
- Despite structural similarity to SENP2, SENP1 exhibits distinct SUMO-processing activities due to these specific interactions.
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