glycine motif
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2018 ◽  
Author(s):  
Silvia C Bobeica ◽  
Shi-Hui Dong ◽  
Liujie Huo ◽  
Nuria Mazo ◽  
Martin I McLaughlin ◽  
...  

2016 ◽  
Vol 113 (14) ◽  
pp. E1983-E1992 ◽  
Author(s):  
Lin Bai ◽  
Kuan Hu ◽  
Tong Wang ◽  
Jordan B. Jastrab ◽  
K. Heran Darwin ◽  
...  

The human pathogen Mycobacterium tuberculosis (Mtb) requires a proteasome system to cause lethal infections in mice. We recently found that proteasome accessory factor E (PafE, Rv3780) activates proteolysis by the Mtb proteasome independently of adenosine triphosphate (ATP). Moreover, PafE contributes to the heat-shock response and virulence of Mtb. Here, we show that PafE subunits formed four-helix bundles similar to those of the eukaryotic ATP-independent proteasome activator subunits of PA26 and PA28. However, unlike any other known proteasome activator, PafE formed dodecamers with 12-fold symmetry, which required a glycine-XXX-glycine-XXX-glycine motif that is not found in previously described activators. Intriguingly, the truncation of the PafE carboxyl-terminus resulted in the robust binding of PafE rings to native proteasome core particles and substantially increased proteasomal activity, suggesting that the extended carboxyl-terminus of this cofactor confers suboptimal binding to the proteasome core particle. Collectively, our data show that proteasomal activation is not limited to hexameric ATPases in bacteria.


2006 ◽  
Vol 20 (4) ◽  
Author(s):  
Francisca E Reyes‐Turcu ◽  
John R Horton ◽  
Xiaodong Cheng ◽  
Keith D Wilkinson

Microbiology ◽  
2004 ◽  
Vol 150 (5) ◽  
pp. 1121-1126 ◽  
Author(s):  
G. Dirix ◽  
P. Monsieurs ◽  
K. Marchal ◽  
J. Vanderleyden ◽  
J. Michiels

1997 ◽  
Vol 11 (1) ◽  
pp. 135-147 ◽  
Author(s):  
Matteo Antorini ◽  
Umberto Breme ◽  
Paolo Caccia ◽  
Cesare Grassi ◽  
Sylvian Lebrun ◽  
...  

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