Identification of Primary and Secondary UBA Footprints on the Surface of Ubiquitin in Cell-mimicking Crowded Solution

Overview

Journal FEBS Lett

Specialty Biochemistry

Date 2017 Mar 8

PMID 28267209

Citations 5

Authors

Francesca Munari

Andrea Bortot

Serena Zanzoni

Mariapina DOnofrio

David Fushman

Michael Assfalg

Affiliations

Soon will be listed here.

Abstract

Despite significant advancements in our understanding of ubiquitin-mediated signaling, the influence of the intracellular environment on the formation of transient ubiquitin-partner complexes remains poorly explored. In our work, we introduce macromolecular crowding as a first level of complexity toward the imitation of a cellular environment in the study of such interactions. Using NMR spectroscopy, we find that the stereospecific complex of ubiquitin and the ubiquitin-associated domain (UBA) is minimally perturbed by the crowding agent Ficoll. However, in addition to the primary canonical recognition patch on ubiquitin, secondary patches are identified, indicating that in cell-mimicking crowded solution, UBA contacts ubiquitin at multiple sites.

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