Work

Chemical protein synthesis combined with protein cell delivery reveals new insights on the maturation process of SUMO2

Year: 2024

Type: article

Abstract: and in live cells. Applying this unique combination we show that SUMO2 analogues containing the native tail undergo rapid cleavage and nuclear localisation, while a Gly93Ala mutation impairs cleavage and alters localisation. Tail mutations (Val94Glu, Tyr95Ala) affected cleavage rates, highlighting roles in SUMO-SENP protease interactions. In cells, SUMO2 analogues containing tail mutations underwent cleavage and subsequently incorporated into promyelocytic leukemia nuclear bodies (PML-NBs). These findings advance our understanding of SUMO2 maturation and provide a foundation for future studies of this process for different SUMO paralogues in various cell lines and tissues.

Source: Chemical Science

DOI: 10.1039/d4sc06254j

Authors: Dana Shkolnik, Subhasis Dey, Mahdi Hasan, Michael J. Matunis, Ashraf Brik

Institutions: Technion – Israel Institute of Technology, Johns Hopkins University

Language: English

Topic: Ubiquitin and proteasome pathways

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: diamond

Funder: United States - Israel Binational Science Foundation

Award: G4770515505