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Literature summary for 2.3.2.8 extracted from

  • Kim, E.; Kim, S.; Lee, J.H.; Kwon, Y.T.; Lee, M.J.
    Ablation of Arg-tRNA-protein transferases results in defective neural tube development (2016), BMB Rep., 49, 443-448 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information generation of ATE1-/- deletion mice. Genotyping of litter embryos at E14.5 retrieved from the ATE+/- intercross reveals no live homozygous mutants, indicating that the deletion of the ATE1 gene is lethal at midgestation. Defective neuronal-cell proliferation in the ATE1-null embryonic brain, overview Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arginyl-tRNAArg + protein Mus musculus
-
tRNAArg + L-arginyl-[protein]
-
?
L-arginyl-tRNAArg + protein Mus musculus 129SvEv/C57BL/6
-
tRNAArg + L-arginyl-[protein]
-
?
L-arginyl-tRNAArg + RGS4 protein Mus musculus
-
tRNAArg + L-arginyl-[RGS4 protein]
-
?
L-arginyl-tRNAArg + RGS4 protein Mus musculus 129SvEv/C57BL/6
-
tRNAArg + L-arginyl-[RGS4 protein]
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus Q9Z2A5
-
-
Mus musculus 129SvEv/C57BL/6 Q9Z2A5
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Mus musculus
-
central nervous system
-
Mus musculus
-
embryo
-
Mus musculus
-
fibroblast MEFs Mus musculus
-
heart
-
Mus musculus
-
additional information expression of ATE1 is prominent in the developing brain and spinal cord, and this pattern overlaps with the migration path of neural stem cells Mus musculus
-
spinal cord
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginyl-tRNAArg + protein
-
Mus musculus tRNAArg + L-arginyl-[protein]
-
?
L-arginyl-tRNAArg + protein
-
Mus musculus 129SvEv/C57BL/6 tRNAArg + L-arginyl-[protein]
-
?
L-arginyl-tRNAArg + RGS4 protein
-
Mus musculus tRNAArg + L-arginyl-[RGS4 protein]
-
?
L-arginyl-tRNAArg + RGS4 protein
-
Mus musculus 129SvEv/C57BL/6 tRNAArg + L-arginyl-[RGS4 protein]
-
?

Synonyms

Synonyms Comment Organism
Arg-transferase
-
Mus musculus
Arg-tRNA-protein transferase
-
Mus musculus
Ate1
-
Mus musculus

General Information

General Information Comment Organism
evolution ATE1 Arg-transferase is an evolutionarily conserved protein present in all eukaryotes from fungi to animals Mus musculus
malfunction ATE1-null mice show severe intracerebral hemorrhages and cystic space near the neural tubes. The ATE1-/- brain shows defective G-protein signaling. Reduced mitosis in ATE1-/- neuroepithelium and a significantly higher nitric oxide concentration in ATE1-/- brain are observed. In ATE1-null murine embryos, neural-tube genesis is severely defective, and this problem may be the primary cause of embryonic mortality of the mutant mice. ATE1 expression is more prominent in the embryonic brain and spinal cord than in the heart. ATE1-null embryonic brain shows stabilized regulators of G protein signaling (RGS) proteins, defective G protein signaling, and a higher concentration of NO. Proliferation of ATE1-/- neuroepithelial cells in the developing primary neural tube is significantly impaired. Stabilized RGS proteins in ATE1-null mice and reduced activities of downstream effectors, overview Mus musculus
metabolism the arginylation branch of the N-end rule pathway is a ubiquitin-mediated proteolytic system in which post-translational conjugation of Arg by ATE1-encoded Arg-tRNA-protein transferase to N-terminal Asp, Glu, or oxidized Cys residues generates essential degradation signals Mus musculus
physiological function ATE1 Arg-transferase is the key enzyme in the Arg/N-end rule pathway. ATE1 is required for degradation of regulators of G protein signaling (RGS) proteins and GPCR signaling, regulation, overview. Essential role of N-terminal arginylation in neural tube development. The crucial role of ATE1 in neural tube development is directly related to proper turn-over of the RGS4 protein, which participate in the oxygen-sensing mechanism in the cells. Degradation of the RGS4 protein by ATE1 is closely associated with the migration or differentiation of neural crest cells during embryogenesis. Neural crest cells migrate into the heart and vessels Mus musculus