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.
Graduate School and Faculty of Pharmaceutical Sciences, Nagoya City University, Nagoya, 467-8603, Japan.
Yoshinori
Y
Uekusa
Keisuke
K
Okawa
Maho
M
Yagi-Utsumi
Olivier
O
Serve
Yuki
Y
Nakagawa
Tsunehiro
T
Mizushima
Hirokazu
H
Yagi
Yasushi
Y
Saeki
Keiji
K
Tanaka
Koichi
K
Kato
D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000378:metabolism*; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D012441:Saccharomyces cerevisiae
D064267:Intrinsically Disordered Proteins; D018832:Molecular Chaperones; C110856:proteasome maturation protein; D046988:Proteasome Endopeptidase Complex