Backbone 1H, 13C, and 15N assignments of yeast Ump1, an intrinsically disordered protein that functions as a proteasome assembly chaperone

Yoshinori Uekusa, Keisuke Okawa, Maho Yagi-Utsumi, Olivier Serve, Yuki Nakagawa, Tsunehiro Mizushima, Hirokazu Yagi, Yasushi Saeki, Keiji Tanaka, Koichi Kato

Research output: Contribution to journalArticle

7 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)383-386
Number of pages4
JournalBiomolecular NMR Assignments
Issue number2
Publication statusPublished - 2014 Oct 1



  • Intrinsically unstructured protein
  • NMR spectroscopy
  • Proteasome assembly
  • Resonance assignment
  • Ump1

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

Cite this