Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1
<p>Abstract</p> <p>Background</p> <p>The proteasome is a multi-subunit protein machine that is the final destination for cellular proteins that have been marked for degradation via an ubiquitin (Ub) chain appendage. These ubiquitylated proteins either bind directly to t...
Main Authors: | Sweredoski Michael J, Gee Marvin, Kolawa Natalie, Gomez Tara A, Deshaies Raymond J |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2011-05-01
|
Series: | BMC Biology |
Online Access: | http://www.biomedcentral.com/1741-7007/9/33 |
Similar Items
-
Solution structure and Rpn1 interaction of the UBL domain of human RNA polymerase II C-terminal domain phosphatase.
by: Ji-Hye Yun, et al.
Published: (2013-01-01) -
Transfer of Ho endonuclease and Ufo1 to the proteasome by the UbL-UbA shuttle protein, Ddi1, analysed by complex formation in vitro.
by: Olga Voloshin, et al.
Published: (2012-01-01) -
Non-Proteasomal UbL-UbA Family of Proteins in Neurodegeneration
by: Salinee Jantrapirom, et al.
Published: (2019-04-01) -
Yeast UBL-UBA proteins have partially redundant functions in cell cycle control
by: Clarke Duncan J, et al.
Published: (2006-12-01) -
Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface
by: Justin W. Chartron, et al.
Published: (2012-12-01)