scholarly journals Enacyloxin IIa, an inhibitor of protein biosynthesis that acts on elongation factor Tu and the ribosome.

1996 ◽  
Vol 15 (10) ◽  
pp. 2604-2611 ◽  
Author(s):  
R. Cetin ◽  
I. M. Krab ◽  
P. H. Anborgh ◽  
R. H. Cool ◽  
T. Watanabe ◽  
...  
Keyword(s):  
Protein Biosynthesis ◽  
Elongation Factor ◽  
Elongation Factor Tu

scholarly journals Elongation factor Tu: a molecular switch in protein biosynthesis

1992 ◽  
Vol 6 (6) ◽  
pp. 683-688 ◽  
Author(s):  
Albert Weijland ◽  
Kim Harmark ◽  
Robbert H. Cool ◽  
Pieter H. Anborgh ◽  
Andrea Parmeggiani
Keyword(s):  
Protein Biosynthesis ◽  
Elongation Factor ◽  
Molecular Switch ◽  
Elongation Factor Tu

scholarly journals Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33

Biology ◽  
2021 ◽  
Vol 10 (11) ◽  
pp. 1171
Author(s):  
Minho Keum ◽  
Dai Ito ◽  
Mi-Seong Kim ◽  
Yuxi Lin ◽  
Kyeong-Hyeon Yoon ◽  
...  
Keyword(s):  
Molecular Chaperones ◽  
Protein Biosynthesis ◽  
Gel Filtration ◽  
Elongation Factor ◽  
Substantial Effect ◽  
Trigger Factor ◽  
Titration Calorimetry ◽  
Elongation Factor Tu ◽  
Regulate Protein ◽  
The Stability

Hsp33, a prokaryotic redox-regulated holding chaperone, has been recently identified to be able to exhibit an unfoldase and aggregase activity against elongation factor Tu (EF-Tu) in its reduced state. In this study, we investigated the effect of elongation factor Ts (EF-Ts) and trigger factor (TF) on Hsp33-mediated EF-Tu unfolding and aggregation using gel filtration, light scattering, circular dichroism, and isothermal titration calorimetry. We found that EF-Tu unfolding and subsequent aggregation induced by Hsp33 were evident even in its complex state with EF-Ts, which enhanced EF-Tu stability. In addition, although TF alone had no substantial effect on the stability of EF-Tu, it markedly amplified the Hsp33-mediated EF-Tu unfolding and aggregation. Collectively, the present results constitute the first example of synergistic unfoldase/aggregase activity of molecular chaperones and suggest that the stability of EF-Tu is modulated by a sophisticated network of molecular chaperones to regulate protein biosynthesis in cells under stress conditions.

Elongation Factor Tu Mutants Expand Amino Acid Tolerance of Protein Biosynthesis System

2007 ◽  
Vol 129 (46) ◽  
pp. 14458-14462 ◽  
Author(s):  
Yoshio Doi ◽  
Takashi Ohtsuki ◽  
Yoshihiro Shimizu ◽  
Takuya Ueda ◽  
Masahiko Sisido
Keyword(s):  
Amino Acid ◽  
Protein Biosynthesis ◽  
Elongation Factor ◽  
Acid Tolerance ◽  
Elongation Factor Tu
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