scholarly journals Far Western blot as a tool for identification of interaction between ribosomal proteins and translation elongation factor 1A

2007 ◽  
Vol 23 (5) ◽  
pp. 379-385
Author(s):  
T. V. Budkevich ◽  
B. S. Negrutskii ◽  
A. V. El'skaya
Keyword(s):  
Western Blot ◽  
Ribosomal Proteins ◽  
Elongation Factor ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
Translation Elongation Factor 1A ◽  
Far Western Blot

scholarly journals Translation elongation factor 2 depletion by siRNA in mouse liver leads to mTOR-independent translational upregulation of ribosomal protein genes

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Maxim V. Gerashchenko ◽  
Mikhail V. Nesterchuk ◽  
Elena M. Smekalova ◽  
Joao A. Paulo ◽  
Piotr S. Kowalski ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Mammalian Cells ◽  
Ribosomal Proteins ◽  
Mouse Liver ◽  
Negative Impact ◽  
Elongation Factor ◽  
Ribosome Profiling ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
Elongation Factor 2

Abstract Due to breakthroughs in RNAi and genome editing methods in the past decade, it is now easier than ever to study fine details of protein synthesis in animal models. However, most of our understanding of translation comes from unicellular organisms and cultured mammalian cells. In this study, we demonstrate the feasibility of perturbing protein synthesis in a mouse liver by targeting translation elongation factor 2 (eEF2) with RNAi. We were able to achieve over 90% knockdown efficacy and maintain it for 2 weeks effectively slowing down the rate of translation elongation. As the total protein yield declined, both proteomics and ribosome profiling assays showed robust translational upregulation of ribosomal proteins relative to other proteins. Although all these genes bear the TOP regulatory motif, the branch of the mTOR pathway responsible for translation regulation was not activated. Paradoxically, coordinated translational upregulation of ribosomal proteins only occurred in the liver but not in murine cell culture. Thus, the upregulation of ribosomal transcripts likely occurred via passive mTOR-independent mechanisms. Impaired elongation sequesters ribosomes on mRNA and creates a shortage of free ribosomes. This leads to preferential translation of transcripts with high initiation rates such as ribosomal proteins. Furthermore, severe eEF2 shortage reduces the negative impact of positively charged amino acids frequent in ribosomal proteins on ribosome progression.

scholarly journals Evidence That Eukaryotic Translation Elongation Factor 1A (eEF1A) Binds the Gcn2 Protein C Terminus and Inhibits Gcn2 Activity

2011 ◽  
Vol 286 (42) ◽  
pp. 36568-36579 ◽  
Author(s):  
Jyothsna Visweswaraiah ◽  
Sebastien Lageix ◽  
Beatriz A. Castilho ◽  
Lara Izotova ◽  
Terri Goss Kinzy ◽  
...  
Keyword(s):  
Protein C ◽  
Elongation Factor ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
Eukaryotic Translation ◽  
C Terminus ◽  
Translation Elongation Factor 1A

New insights on the interaction between the isoforms 1 and 2 of human translation elongation factor 1A

Biochimie ◽  
2015 ◽  
Vol 118 ◽  
pp. 1-7 ◽  
Author(s):  
Nunzia Migliaccio ◽  
Immacolata Ruggiero ◽  
Nicola M. Martucci ◽  
Carmen Sanges ◽  
Salvatore Arbucci ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
Translation Elongation Factor 1A

scholarly journals Inappropriate expression of the translation elongation factor 1A disrupts genome stability and metabolism

2016 ◽  
Vol 129 (24) ◽  
pp. 4455-4465 ◽  
Author(s):  
Daniel J. Tarrant ◽  
Mariarita Stirpe ◽  
Michelle Rowe ◽  
Mark J. Howard ◽  
Tobias von der Haar ◽  
...  
Keyword(s):  
Genome Stability ◽  
Elongation Factor ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
Inappropriate Expression ◽  
Translation Elongation Factor 1A
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