Protein elongation variant of PUF60 : Milder phenotypic end of the Verheij syndrome

2020 ◽  
Vol 182 (11) ◽  
pp. 2709-2714
Author(s):  
Mamiko Yamada ◽  
Tomoko Uehara ◽  
Hisato Suzuki ◽  
Toshiki Takenouchi ◽  
Kenjiro Kosaki
Keyword(s):  
Protein Elongation

Protein elongation rates in tissues of growing and adult sheep1

2008 ◽  
Vol 86 (9) ◽  
pp. 2288-2295 ◽  
Author(s):  
M. T. Connors ◽  
D. P. Poppi ◽  
J. P. Cant
Keyword(s):  
Protein Elongation

Protein elongation factor EEF1A2 is a putative oncogene in ovarian cancer

10.1038/ng904 ◽  
2002 ◽  
Vol 31 (3) ◽  
pp. 301-305 ◽  
Author(s):  
Nisha Anand ◽  
Sabita Murthy ◽  
Gudrun Amann ◽  
Meredith Wernick ◽  
Lisa A. Porter ◽  
...  
Keyword(s):  
Ovarian Cancer ◽  
Elongation Factor ◽  
Protein Elongation

scholarly journals Transcription and translation in an RNA world

2006 ◽  
Vol 361 (1474) ◽  
pp. 1751-1760 ◽  
Author(s):  
William R Taylor
Keyword(s):  
Amino Acid ◽  
Active Site ◽  
Rna World ◽  
Large Subunit ◽  
Trna Synthetase ◽  
Nucleoside Triphosphate ◽  
Amino Acid Binding ◽  
World Hypothesis ◽  
Protein Elongation ◽  
Rna World Hypothesis

The RNA world hypothesis requires a ribozyme that was an RNA-directed RNA polymerase (ribopolymerase). If such a replicase makes a reverse complementary copy of any sequence (including itself), in a simple RNA world, there is no mechanism to prevent self-hybridization. It is proposed that this can be avoided through the synthesis of a parallel complementary copy. The logical consequences of this are pursued and developed in a computer simulation, where the behaviour of the parallel copy is compared to the conventional reverse complementary copy. It is found that the parallel copy is more efficient at higher temperatures (up to 90°C). A model for the ribopolymerase, based on the core of the large subunit (LSU) of the ribosome, is described. The geometry of a potential active site for this ribopolymerase suggests that it contained a cavity (now occupied by the aminoacyl-tRNA) and that an amino acid binding in this might have ‘poisoned’ the ribopolymerase by cross-reacting with the nucleoside-triphosphate before polymerization could occur. Based on a similarity to the active site components of the class-I tRNA synthetase enzymes, it is proposed that the amino acid could become attached to the nascent RNA transcript producing a variety of aminoacylated tRNA-like products. Using base-pairing interactions, some of these molecules might cross-link two ribopolymerases, giving rise to a precursor of the modern ribosome. A hybrid dimer, half polymerase and half proto-ribosome, could account for mRNA translocation before the advent of protein elongation factors.

Protein Elongation, Co-translational Folding and Targeting

2016 ◽  
Vol 428 (10) ◽  
pp. 2165-2185 ◽  
Author(s):  
Marina V. Rodnina ◽  
Wolfgang Wintermeyer
Keyword(s):  
Protein Elongation

The possible interaction of CDA14 and protein elongation factor 1α

2008 ◽  
Vol 1784 (2) ◽  
pp. 312-318 ◽  
Author(s):  
Ying-Fang Yang ◽  
Min-Yuan Chou ◽  
Chia-Yu Fan ◽  
Sung-Fang Chen ◽  
Ping-Chiang Lyu ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Elongation Factor 1Α ◽  
Protein Elongation

Expression of protein elongation factor eEF1A2 predicts favorable outcome in breast cancer

2006 ◽  
Vol 102 (1) ◽  
pp. 31-41 ◽  
Author(s):  
Geeta Kulkarni ◽  
Dmitry A. Turbin ◽  
Anahita Amiri ◽  
Sujeeve Jeganathan ◽  
Miguel A. Andrade-Navarro ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Elongation Factor ◽  
Favorable Outcome ◽  
Protein Elongation

scholarly journals Plitidepsin, an inhibitor of the cell elongation factor eEF1a, and molnupiravir an analogue of the ribonucleoside cytidine, two new chemical compounds with intense activity against SARS-CoV-2

2021 ◽  
Author(s):  
Jordi Reina ◽  
Keyword(s):  
Elongation Factor ◽  
Chemical Compounds ◽  
Cellular Protein ◽  
Lethal Mutagenesis ◽  
Good Target ◽  
Therapeutic Possibility ◽  
Intense Activity ◽  
Protein Elongation ◽  
Natural Inhibitors ◽  
Replicative Cycle

The knowledge of the replicative cycle of SARS-CoV-2 and its interactions with cellular proteins has opened a new therapeutic possibility based on blocking those essential for the virus. The cellular protein elongation factor eEF1A could be a good target. Among its natural inhibitors are didemnins and their related chemical compounds such as plitidepsin. In human cell culture, this compound is capable of inhibiting the virus with a potency 27,5 times that of remdesivir. It must be administered intravenously. Of the ribonucleoside analogues, molnupiravir (MK-4483/EIDD-2801) (hydroxy-cytidine) determines a lethal mutagenesis on SARS-CoV-2. In animals, after oral administration, the pulmonary viral load decreases 25,000 times and when administered as prophylaxis, approximately 100,000 times. It prevents the transmission of the virus and eliminates its presence in the oropharynx. Both chemicals have started Phase I / II human clinical trials

scholarly journals Differential bicodon usage in lowly and highly abundant proteins

PeerJ ◽  
2017 ◽  
Vol 5 ◽  
pp. e3081 ◽  
Author(s):  
Luis A. Diambra
Keyword(s):  
Codon Usage ◽  
Drug Transport ◽  
Heterologous Gene Expression ◽  
Elongation Rate ◽  
Translation Elongation ◽  
Synonymous Codons ◽  
Domains Of Life ◽  
Small Change ◽  
Protein Elongation ◽  
Codon Pairs

Degeneracy in the genetic code implies that different codons can encode the same amino acid. Usage preference of synonymous codons has been observed in all domains of life. There is much evidence suggesting that this bias has a major role on protein elongation rate, contributing to differential expression and to co-translational folding. In addition to codon usage bias, other preference variations have been observed such as codon pairs. In this paper, I report that codon pairs have significant different frequency usage for coding either lowly or highly abundant proteins. These usage preferences cannot be explained by the frequency usage of the single codons. The statistical analysis of coding sequences of nine organisms reveals that in many cases bicodon preferences are shared between related organisms. Furthermore, it is observed that misfolding in the drug-transport protein, encoded by MDR1 gene, is better explained by a big change in the pause propensity due to the synonymous bicodon variant, rather than by a relatively small change in codon usage. These findings suggest that codon pair usage can be a more powerful framework to understand translation elongation rate, protein folding efficiency, and to improve protocols to optimize heterologous gene expression.

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