Genetically Encoded Crosslinking Enables Identification of Multivalent Ubiquitin‐Deubiquitylating Enzyme Interactions

Author:

Patel Rishi1ORCID,Negrón Terón Kristos1,Zhou Mowei2,Nakayasu Ernesto3,Drown Bryon1,Das Chittaranjan1ORCID

Affiliation:

1. Department of Chemistry Purdue University 560 Oval Dr. West Lafayette IN 47907 USA

2. Environmental and Molecular Sciences Division Pacific Northwest National Laboratory 902 Battelle Blvd Richland WA 99352 USA

3. Biological Sciences Division Pacific Northwest National Laboratory 902 Battelle Blvd Richland WA 99352 USA

Abstract

AbstractUbiquitin (Ub) proteoforms control nearly every aspect of eukaryotic cell biology through their diversity. Inspired by the widely used Ub C‐terminal electrophiles (Ub−E), here we report the identification of multivalent binding of Ub with deubiquitylating enzymes (Dubs) using genetic code expansion (GCE) and crosslinking mass spectrometry. While the Ub−Es only gather structural information with the S1 Dub sites, we demonstrate that GCE of Ub with p‐benzoyl‐L‐phenylalanine enables identification of interaction modes beyond the S1 site with a panel of Dubs of both eukaryotic and prokaryotic origin. Collectively, this represents the next generation of Ub‐based affinity probes with a unique ability to unravel Ub interaction landscapes beyond what is afforded by cysteine‐based chemistries.

Funder

U.S. Department of Energy

National Institute of General Medical Sciences

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

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