scholarly journals Functional Role of Tia1/Pub1 and Sup35 Prion Domains: Directing Protein Synthesis Machinery to the Tubulin Cytoskeleton

2014 ◽  
Vol 55 (2) ◽  
pp. 305-318 ◽  
Author(s):  
Xiang Li ◽  
Joseph B. Rayman ◽  
Eric R. Kandel ◽  
Irina L. Derkatch
Cell ◽  
1989 ◽  
Vol 57 (4) ◽  
pp. 525-529 ◽  
Author(s):  
Albert E. Dahlberg

2012 ◽  
Vol 419 (3-4) ◽  
pp. 125-138 ◽  
Author(s):  
Xinying Shi ◽  
Prashant K. Khade ◽  
Karissa Y. Sanbonmatsu ◽  
Simpson Joseph

2015 ◽  
Vol 112 (14) ◽  
pp. 4310-4315 ◽  
Author(s):  
Richard D. Bunker ◽  
Kalyaneswar Mandal ◽  
Ghader Bashiri ◽  
Jessica J. Chaston ◽  
Bradley L. Pentelute ◽  
...  

Protein 3D structure can be a powerful predictor of function, but it often faces a critical roadblock at the crystallization step. Rv1738, a protein from Mycobacterium tuberculosis that is strongly implicated in the onset of nonreplicating persistence, and thereby latent tuberculosis, resisted extensive attempts at crystallization. Chemical synthesis of the l- and d-enantiomeric forms of Rv1738 enabled facile crystallization of the d/l-racemic mixture. The structure was solved by an ab initio approach that took advantage of the quantized phases characteristic of diffraction by centrosymmetric crystals. The structure, containing l- and d-dimers in a centrosymmetric space group, revealed unexpected homology with bacterial hibernation-promoting factors that bind to ribosomes and suppress translation. This suggests that the functional role of Rv1738 is to contribute to the shutdown of ribosomal protein synthesis during the onset of nonreplicating persistence of M. tuberculosis.


2009 ◽  
Vol 221 (03) ◽  
Author(s):  
B Steiger ◽  
I Leuschner ◽  
D Denkhaus ◽  
D von Schweinitz ◽  
T Pietsch
Keyword(s):  

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