NMR characterization of the interaction between the PUB domain of peptide:N-glycanase and ubiquitin-like domain of HR23

FEBS Letters
Yukiko KamiyaKoichi Kato

Abstract

PUB domains are identified in several proteins functioning in the ubiquitin (Ub)-proteasome system and considered as p97-binding modules. To address the further functional roles of these domains, we herein characterized the interactions of the PUB domain of peptide:N-glycanase (PNGase) with Ub and Ub-like domain (UBL) of the proteasome shuttle factor HR23. NMR data indicated that PNGase-PUB exerts an acceptor preferentially for HR23-UBL, electrostatically interacting with the UBL surface employed for binding to other Ub/UBL motifs. Our findings imply that PNGase-PUB serves not only as p97-binding module but also as a possible activator of HR23 in endoplasmic reticulum-associated degradation mechanisms.

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Citations

Mar 22, 2014·Genetics in Medicine : Official Journal of the American College of Medical Genetics·Gregory M EnnsDavid B Goldstein
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Apr 15, 2014·Molecular Cell·Paul R ElliottDavid Komander
Jan 9, 2015·Chemical Communications : Chem Comm·Sota SatoMakoto Fujita

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