Backbone 1H, 13C, and 15N assignments of yeast Ump1, an intrinsically disordered protein that functions as a proteasome assembly chaperone
Eukaryotic proteasome assembly is a highly organized process mediated by several proteasome-specific chaperones, which interact with proteasome assembly intermediates. In yeast, Ump1 and Pba1-4 have been identified as assembly chaperones that are dedicated to the formation of the proteasome 20S catalytic core complex. The crystal structures of Pba chaperones have been reported previously, but no detailed information has been provided for the structure of Ump1. Thus, to better understand the mechanisms underlying Ump1-mediated proteasome assembly, we characterized the conformation of Ump1 in solution using NMR. Backbone chemical shift data indicated that Ump1 is an intrinsically unstructured protein and largely devoid of secondary structural elements.
KeywordsUmp1 Intrinsically unstructured protein Proteasome assembly NMR spectroscopy Resonance assignment
We would like to thank Ms. Kumiko Hattori and Ms. Kiyomi Senda (Nagoya City University) for their help with recombinant protein preparation. We also thank Dr. Takumi Yamaguchi and Ms. Michiko Nakano for their help with NMR measurements. This work was supported in part by JSPS Grants-in-Aid for Scientific Research on Innovative Areas (25102008 to K. K.), by the Okazaki ORION project, and by the Nanotechnology Platform Project and the Targeted Proteins Research Program from the Ministry of Education, Culture, Sports, Science and Technology (to K. T. and K. K.).
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