Identification of primary and secondary UBA footprints on the surface of ubiquitin in cell-mimicking crowded solution.
Identification of primary and secondary UBA footprints on the surface of ubiquitin in cell-mimicking crowded solution.
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DOI：
10.1002/1873-3468.12615
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发表时间：
2017-04
期刊：
影响因子：
3.5
通讯作者：
Assfalg M
中科院分区：
文献类型：
--
作者：
Munari F;Bortot A;Zanzoni S;D'Onofrio M;Fushman D;Assfalg M
Despite significant advancements in our understanding of ubiquitin-mediated signaling, the influence of the intracellular environment on formation of transient ubiquitin-partner complexes remains poorly explored. In our work, we introduce macromolecular crowding as a first level of complexity towards the imitation of a cellular environment in the study of such interactions. Using NMR spectroscopy, we find that the stereospecific complex of ubiquitin and 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.
