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.

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

The stability of mRNA for eucaryotic elongation factor Tu in Friend erythroleukemia cells varies with growth rate

1988 ◽  
Vol 8 (3) ◽  
pp. 1085-1092
Author(s):  
T R Rao ◽  
L I Slobin
Keyword(s):  
Stationary Phase ◽  
Mrna Decay ◽  
Elongation Factor ◽  
Growth Conditions ◽  
Decay Rates ◽  
Fresh Medium ◽  
Initiation Factor ◽  
Elongation Factor Tu ◽  
Messenger Ribonucleoprotein ◽  
The Stability

The decay rates of eucaryotic elongation factor Tu (eEF-Tu) mRNA and eucaryotic initiation factor 4A (eIF-4A) mRNA in Friend erythroleukemia (FEL) cells were determined under several different growth conditions. In FEL cells which were no longer actively dividing (stationary phase), eEF-Tu mRNA was found to be rather stable, with a t1/2 of about 24 h. In rapidly growing FEL cells eEF-Tu mRNA was considerably less stable, with a t1/2 of about 9 h. In both cases a single rate of mRNA decay was observed. However, when stationary-phase cells resumed growth after treatment with fresh medium, we observed that eEF-Tu mRNA decay followed a biphasic process. The faster of the two decay rates involved approximately 50% of the eEF-Tu mRNA and had a t1/2 of about 1 h. The decay rates for eIF-4A (t1/2 = 2 h) and total poly(A)+ RNA (t1/2 = 3 h) were unaffected by changes in growth conditions. The t1/2 for polysomal eEF-Tu mRNA was found to be about 8 h when stationary FEL cells were treated with fresh medium. Previous work in this laboratory has shown (T. R. Rao and L. I. Slobin, Mol. Cell. Biol. 7:687-697, 1987) that when FEL cells are allowed to grow to stationary phase, approximately 60% of the mRNA for eEF-Tu is found in a nontranslating postpolysomal messenger ribonucleoprotein (mRNP) particle. eEF-Tu mRNP was rapidly cleared from stationary cells after treatment with fresh medium. The data presented in this report indicate that the stability of eEF-Tu mRNP is rapidly altered and the particle is targeted for degradation when stationary FEL cells resume growth.

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 The stability of mRNA for eucaryotic elongation factor Tu in Friend erythroleukemia cells varies with growth rate.

1988 ◽  
Vol 8 (3) ◽  
pp. 1085-1092 ◽  
Author(s):  
T R Rao ◽  
L I Slobin
Keyword(s):  
Stationary Phase ◽  
Mrna Decay ◽  
Elongation Factor ◽  
Growth Conditions ◽  
Decay Rates ◽  
Fresh Medium ◽  
Initiation Factor ◽  
Elongation Factor Tu ◽  
Messenger Ribonucleoprotein ◽  
The Stability

The decay rates of eucaryotic elongation factor Tu (eEF-Tu) mRNA and eucaryotic initiation factor 4A (eIF-4A) mRNA in Friend erythroleukemia (FEL) cells were determined under several different growth conditions. In FEL cells which were no longer actively dividing (stationary phase), eEF-Tu mRNA was found to be rather stable, with a t1/2 of about 24 h. In rapidly growing FEL cells eEF-Tu mRNA was considerably less stable, with a t1/2 of about 9 h. In both cases a single rate of mRNA decay was observed. However, when stationary-phase cells resumed growth after treatment with fresh medium, we observed that eEF-Tu mRNA decay followed a biphasic process. The faster of the two decay rates involved approximately 50% of the eEF-Tu mRNA and had a t1/2 of about 1 h. The decay rates for eIF-4A (t1/2 = 2 h) and total poly(A)+ RNA (t1/2 = 3 h) were unaffected by changes in growth conditions. The t1/2 for polysomal eEF-Tu mRNA was found to be about 8 h when stationary FEL cells were treated with fresh medium. Previous work in this laboratory has shown (T. R. Rao and L. I. Slobin, Mol. Cell. Biol. 7:687-697, 1987) that when FEL cells are allowed to grow to stationary phase, approximately 60% of the mRNA for eEF-Tu is found in a nontranslating postpolysomal messenger ribonucleoprotein (mRNP) particle. eEF-Tu mRNP was rapidly cleared from stationary cells after treatment with fresh medium. The data presented in this report indicate that the stability of eEF-Tu mRNP is rapidly altered and the particle is targeted for degradation when stationary FEL cells resume growth.

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

scholarly journals Binding Interaction between Tet(M) and the Ribosome: Requirements for Binding

1998 ◽  
Vol 180 (16) ◽  
pp. 4089-4092 ◽  
Author(s):  
Kathi A. Dantley ◽  
H. Kathleen Dannelly ◽  
Vickers Burdett
Keyword(s):  
Complex Formation ◽  
Protein Biosynthesis ◽  
Gel Filtration ◽  
Resistance Mechanism ◽  
Elongation Factor ◽  
M Protein ◽  
Binding Interaction ◽  
Gtp Hydrolysis ◽  
Direct Competition ◽  
Factor G

ABSTRACT Tet(M) protein interacts with the protein biosynthesis machinery to render this process resistant to tetracycline by a mechanism which involves release of the antibiotic from the ribosome in a reaction dependent on GTP hydrolysis. To clarify this resistance mechanism further, the interaction of Tet(M) with the ribosome has been examined by using a gel filtration assay with radioactively labelled Tet(M) protein. The presence of GTP and 5′-guanylyl imido diphosphate, but not GDP, promoted Tet(M)-ribosome complex formation. Furthermore, thiostrepton, which inhibits the activities of elongation factor G (EF-G) and EF-Tu by binding to the ribosome, blocks stable Tet(M)-ribosome complex formation. Direct competition experiments show that Tet(M) and EF-G bind to overlapping sites on the ribosome.

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