Ricin A-Chain Substrate Specificity in RNA, DNA, and Hybrid Stem−Loop Structures†

Biochemistry ◽  
2004 ◽  
Vol 43 (17) ◽  
pp. 4913-4922 ◽  
Author(s):  
Tim K. Amukele ◽  
Vern L. Schramm
Toxicon ◽  
1996 ◽  
Vol 34 (11-12) ◽  
pp. 1317-1324 ◽  
Author(s):  
Todd Link ◽  
Xiang Yang Chen ◽  
Lin Hao Niu ◽  
Vern L. Schramm

Biochemistry ◽  
1998 ◽  
Vol 37 (33) ◽  
pp. 11605-11613 ◽  
Author(s):  
Xiang-Yang Chen ◽  
Todd M. Link ◽  
Vern L. Schramm
Keyword(s):  
A Chain ◽  

2006 ◽  
Vol 172 (2) ◽  
pp. 211-219 ◽  
Author(s):  
Ikjin Kim ◽  
Jungmi Ahn ◽  
Chang Liu ◽  
Kaori Tanabe ◽  
Jennifer Apodaca ◽  
...  

Misfolded proteins in the endoplasmic reticulum (ER) are destroyed by a pathway termed ER-associated protein degradation (ERAD). Glycans are often removed from glycosylated ERAD substrates in the cytosol before substrate degradation, which maintains the efficiency of the proteasome. Png1, a deglycosylating enzyme, has long been suspected, but not proven, to be crucial in this process. We demonstrate that the efficient degradation of glycosylated ricin A chain requires the Png1–Rad23 complex, suggesting that this complex couples protein deglycosylation and degradation. Rad23 is a ubiquitin (Ub) binding protein involved in the transfer of ubiquitylated substrates to the proteasome. How Rad23 achieves its substrate specificity is unknown. We show that Rad23 binds various regulators of proteolysis to facilitate the degradation of distinct substrates. We propose that the substrate specificity of Rad23 and other Ub binding proteins is determined by their interactions with various cofactors involved in specific degradation pathways.


Biochemistry ◽  
2005 ◽  
Vol 44 (11) ◽  
pp. 4416-4425 ◽  
Author(s):  
Tim K. Amukele ◽  
Setu Roday ◽  
Vern L. Schramm

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