NDLI: $^{1}$H, $^{13}$C and $^{15}$N resonance assignments of Rpn9, a regulatory subunit of 26S proteasome from Saccharomyces cerevisiae

Content Provider	Springer Nature Link
Author	Wu, Yujie Hu, Yunfei Jin, Changwen
Copyright Year	2013
Abstract	The 26S proteasome is an essential molecular machine for specific protein degradation in eukaryotic cells. The 26S proteasome is formed by a central 20S core particle capped by two 19S regulatory particle (RP) at both ends. The Rpn9 protein is a non-ATPase subunit located in the lid complex of the 19S RP, and is identified to be essential for efficient assembly of yeast 26S proteasome. Bioinformatics analysis of Saccharomyces cerevisiae Rpn9 suggested it contains a PCI domain at the C-terminal region. However, high-resolution structures of either the PCI domain or the full-length Rpn9 still remain elusive. Herein, we report the chemical shift assignments of $^{1}$H, $^{13}$C and $^{15}$N atoms of the individual N- and C-domains, as well as full-length S. cerevisiae Rpn9, which provide the basis for further structural and functional studies of Rpn9 using solution NMR technique.
Starting Page	307
Ending Page	311
Page Count	5
File Format	PDF
ISSN	18742718
Journal	Biomolecular NMR Assignments
Volume Number	8
Issue Number	2
e-ISSN	1874270X
Language	English
Publisher	Springer Netherlands
Publisher Date	2013-07-06
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Proteasome Rpn9 PCI NMR Assignments Biophysics and Biological Physics Polymer Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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$^{1}$H, $^{13}$C and $^{15}$N resonance assignments of Rpn9, a regulatory subunit of 26S proteasome from Saccharomyces cerevisiae