Arginyl-tRNA transferase activity as a maker of cellular aging in peripheral rat tissues

@article{Lamon1980ArginyltRNATA,
  title={Arginyl-tRNA transferase activity as a maker of cellular aging in peripheral rat tissues},
  author={Kim D. Lamon and Hideko Kaji},
  journal={Experimental Gerontology},
  year={1980},
  volume={15},
  pages={53-64}
}
  • K. Lamon, H. Kaji
  • Published 31 December 1980
  • Biology, Chemistry
  • Experimental Gerontology
View on Elsevier
doi.org
17 Citations
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17 Citations

Ablation of arginyl‐tRNA‐protein transferase in oligodendrocytes impairs central nervous system myelination
TLDR
It is demonstrated that Ate1 helps maintain proper OL differentiation and myelination in corpus callosum in vivo, and that protein arginylation plays an essential role in developmental myelinations.
Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo.
Transfer ribonucleic acid dependent but ribosome-independent leucine incorporation into rat brain protein.
TLDR
An unusual type of posttranslational modification has been observed in a rat brain in vitro system and it is proposed that an ester bond is formed between the leucine and the side chain of a serine, threonine, or tyrosine in the acceptor protein.
Activity patterns of aminoacyl-tRNA synthetases, tRNA methylases, arginyltransferase and tubulin: tyrosine ligase during development and ageing of Caenorhabditis elegans.
TLDR
The results are consistent with the idea of a modulation of protein synthesis and other cellular processes by quantitative activity changes during development and ageing.
Complete purification of arginyl-tRNA:protein arginyltransferase from hog kidney and production of its antibody.
Biochemical analysis of protein arginylation.
Protein Arginylation, a Global Biological Regulator that Targets Actin Cytoskeleton and the Muscle
TLDR
An overview of the studies of protein arginylation that led to the discovery of its major role in the muscle is presented, and follow up studies strongly suggests that arkinylation constitutes a novel biological regulator of contractility.
Posttranslational arginylation as a global biological regulator.
Protein Arginylation: Over 50 Years of Discovery.
  • A. Kashina
  • Biology, Chemistry
    Methods in molecular biology
  • 2015
TLDR
This chapter contains an overview of all the major milestones in the protein arginylation field, from its original discovery in 1963 to this day.
Heat stress induced arginylation of HuR promotes alternative polyadenylation of Hsp70.3 by regulating HuR stability and RNA binding
TLDR
In conclusion, arginylation dependent modifications of HuR maintained its cellular homeostasis, and promoted APA of Hsp70.3 pre-mRNA, during early HS response.
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References

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TLDR
Observations suggest that aminoacyl-transferase may function in the modification of chromosomal proteins and that modification of chromatin may alter the regulatory mechanisms of cellular functions.
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TLDR
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Abstract The arginyl transfer ribonucleic acid-protein transferase has been purified nearly 7000-fold from the supernatant fraction of rabbit liver cytoplasm by a procedure including ammonium sulfate…
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