Modifying the Vicinity of the Isopeptide Bond To Reveal Differential Behavior of Ubiquitin Chains with Interacting Proteins: Organic Chemistry Applied to Synthetic Proteins

Authors


  • This work was supported by the Israel Science foundation (A.B.) and the NIH grant GM065334 (D.F.). M.P. gratefully acknowledges the Azrieli Foundation for financial support. Research in the laboratory of A.C. is supported by grants from the Dr. Miriam and Sheldon G. Adelson Medical Research Foundation (AMRF), the I-CORE Program of the Planning and Budgeting Committee, the Israel Science Foundation (ISF) (grant no. 1775/12), The TreatPolyQ Network funded by the EU, and the Deutsch-Israelische Projektkooperation (DIP). A.C. is an Israel Cancer Research Fund (ICRF) USA Professor.

Abstract

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In every direction: Chemical protein synthesis allows the construction of 14 di-ubiquitin analogues modified in the vicinity of the isopeptide bond to examine their behavior with deubiquitinases and ubiquitin binding domains. The results set the ground for the generation of unique probes for studying the interactions of these chains with various ubiquitin-interacting proteins.

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