Disentangling the recognition complexity of a protein hub using a nanopore

Lauren Ashley Mayse, Ali Imran, Motahareh Ghahari Larimi, Michael S. Cosgrove, Aaron James Wolfe and Liviu Movileanu ()
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Lauren Ashley Mayse: Syracuse University
Ali Imran: Syracuse University
Motahareh Ghahari Larimi: Syracuse University
Michael S. Cosgrove: State University of New York - Upstate Medical University, 4249 Weiskotten Hall
Aaron James Wolfe: Syracuse University
Liviu Movileanu: Syracuse University

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract WD40 repeat proteins are frequently involved in processing cell signaling and scaffolding large multi-subunit machineries. Despite their significance in physiological and disease-like conditions, their reversible interactions with other proteins remain modestly examined. Here, we show the development and validation of a protein nanopore for the detection and quantification of WD40 repeat protein 5 (WDR5), a chromatin-associated hub involved in epigenetic regulation of histone methylation. Our nanopore sensor is equipped with a 14-residue Win motif of mixed lineage leukemia 4 methyltransferase (MLL4Win), a WDR5 ligand. Our approach reveals a broad dynamic range of MLL4Win-WDR5 interactions and three distant subpopulations of binding events, representing three modes of protein recognition. The three binding events are confirmed as specific interactions using a weakly binding WDR5 derivative and various environmental contexts. These outcomes demonstrate the substantial sensitivity of our nanopore sensor, which can be utilized in protein analytics.

Date: 2022
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DOI: 10.1038/s41467-022-28465-8

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