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Literature summary for 2.3.2.8 extracted from
- Posttranslational arginylation enzyme Ate1 affects DNA mutagenesis by regulating stress response (2016), Cell Death Dis., 7, e2378 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ate1, single copy gene | Saccharomyces cerevisiae |
| gene ate1, single copy gene | Mus musculus |
| gene ate1, single copy gene | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| malfunction | knockout of ATE1 gene in MEFs significantly reduces apoptotic rates in the presence of microbial alkaloid toxin staurosporine (STS) compared to wild-type. Similar results are observed with a different stressor, CdCl2 | Mus musculus |
| additional information | generation of ate1 knockout fibroblasts | Homo sapiens |
| additional information | knockout or knockdown of ATE1 decreasing cellular sensitivity towards stressing conditions, e.g. heat, high NaCl, or H2O2 | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-arginyl-tRNAArg + protein | Saccharomyces cerevisiae | - |
tRNAArg + L-arginyl-[protein] | - |
? |  |
| L-arginyl-tRNAArg + protein | Mus musculus | - |
tRNAArg + L-arginyl-[protein] | - |
? | |
| L-arginyl-tRNAArg + protein | Homo sapiens | - |
tRNAArg + L-arginyl-[protein] | - |
? | |
| L-arginyl-tRNAArg + protein | Saccharomyces cerevisiae BY4741 | - |
tRNAArg + L-arginyl-[protein] | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | O95260 | - |
- |
| Mus musculus | Q9Z2A5 | - |
- |
| Saccharomyces cerevisiae | - |
- |
- |
| Saccharomyces cerevisiae BY4741 | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| embryonic fibroblast | MEF | Mus musculus | - |
| foreskin fibroblast cell line | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-arginyl-tRNAArg + protein | - |
Saccharomyces cerevisiae | tRNAArg + L-arginyl-[protein] | - |
? | |
| L-arginyl-tRNAArg + protein | - |
Mus musculus | tRNAArg + L-arginyl-[protein] | - |
? | |
| L-arginyl-tRNAArg + protein | - |
Homo sapiens | tRNAArg + L-arginyl-[protein] | - |
? | |
| L-arginyl-tRNAArg + protein | - |
Saccharomyces cerevisiae BY4741 | tRNAArg + L-arginyl-[protein] | - |
? | |
| additional information | usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts | Saccharomyces cerevisiae | ? | - |
- |
|
| additional information | usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts | Mus musculus | ? | - |
- |
|
| additional information | usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts | Homo sapiens | ? | - |
- |
|
| additional information | usage of DD-bta15-GFP assay for an 'in-lysate' reaction to examine arginylation activity in cell extracts | Saccharomyces cerevisiae BY4741 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| arginyltransferase 1 | - |
Saccharomyces cerevisiae |
| arginyltransferase 1 | - |
Mus musculus |
| arginyltransferase 1 | - |
Homo sapiens |
| Ate1 | - |
Saccharomyces cerevisiae |
| Ate1 | - |
Mus musculus |
| Ate1 | - |
Homo sapiens |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Mus musculus | Ate1 and arginylation are upregulated during stress and are responsible for cell death, stress is caused by e.g. H2O2, CdCl2, heat, high salt, or staurosporine, overview | up |
| Homo sapiens | Ate1 and arginylation are upregulated during stress and are responsible for cell death, stress is caused by e.g. H2O2, CdCl2, heat, high salt, or staurosporine, overview | up |
| Saccharomyces cerevisiae | Ate1 and arginylation are upregulated during stress and are responsible for cell death, stress is caused by e.g. H2O2, CdCl2, heat, high salt, or staurosporine. In wild-type cells responding to stress, there is an increase of cellular Ate1 protein level and arginylation activity, overview. The increase of Ate1 protein directly promotes cell death in a manner dependent on its arginylation activity. The wild-type and ate1DELTA yeast are challenged with high-temperature conditions: at 40°C, a heat-stress temperature for yeast, the mutant ate1DELTA yeast grows significantly faster than the wild-type. Buut when these yeast cultures are transferred from 40°C to room temperature, a non-stressing temperature for recovery, similar numbers of colonies eventually form in both the ate1DELTA and wild-type yeast. This suggests that both yeast strains are equally viable, and their difference in growth at 40°C is mainly due to a difference in growth arrest | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | eukaryotic systems including Saccharomyces cerevisiae (budding yeast), mouse cells, and human cells, all contain the evolutionarily conserved ATE1 gene | Saccharomyces cerevisiae |
| evolution | eukaryotic systems including Saccharomyces cerevisiae (budding yeast), mouse cells, and human cells, all contain the evolutionarily conserved ATE1 gene | Mus musculus |
| evolution | eukaryotic systems including Saccharomyces cerevisiae (budding yeast), mouse cells, and human cells, all contain the evolutionarily conserved ATE1 gene | Homo sapiens |
| malfunction | deletion or downregulation of the ATE1 gene disrupts typical stress responses by bypassing growth arrest and suppressing cell death events in the presence of disease-related stressing factors, including oxidative, heat, and osmotic stresses, as well as the exposure to heavy metals or radiation. Conversely, in wild-type cells responding to stress, there is an increase of cellular Ate1 protein level and arginylation activity. The faster growth rates of ate1DELTA mutant yeast in stressing condition compared to wild-type is likely caused by a lack of growth arrest | Saccharomyces cerevisiae |
| malfunction | knockout of ATE1 gene in MEFs significantly reduces apoptotic rates in the presence of microbial alkaloid toxin staurosporine (STS) compared to wild-type. Similar results are observed with a different stressor, CdCl2 | Mus musculus |
| metabolism | link between Ate1 and a variety of diseases including cancer | Saccharomyces cerevisiae |
| metabolism | link between Ate1 and a variety of diseases including cancer | Mus musculus |
| metabolism | link between Ate1 and a variety of diseases including cancer | Homo sapiens |
| physiological function | arginyltransferase 1 (Ate1) mediates protein arginylation, a protein posttranslational modification (PTM) in eukaryotic cells. Ate1 is required to suppress mutation frequency in yeast and mammalian cells during DNA-damaging conditions such as ultraviolet irradiation. Ate1 and arginylation are upregulated during stress and are responsible for cell death, role of Ate1/arginylation in stress response, overview. Ate1 is essential for the suppression of mutagenesis during DNA-damaging stress. Growth arrest and cell death during stress could be interpreted as a mechanism to prevent incorporation of damaged genetic material or transmission of mutation to the subsequent generations | Saccharomyces cerevisiae |
| physiological function | arginyltransferase 1 (Ate1) mediates protein arginylation, a protein posttranslational modification (PTM) in eukaryotic cells. Ate1 is required to suppress mutation frequency in yeast and mammalian cells during DNA-damaging conditions such as ultraviolet irradiation. Ate1 and arginylation are upregulated during stress and are responsible for cell death, role of Ate1/arginylation in stress response, overview. Ate1 is essential for the suppression of mutagenesis during DNA-damaging stress. Growth arrest and cell death during stress could be interpreted as a mechanism to prevent incorporation of damaged genetic material or transmission of mutation to the subsequent generations | Mus musculus |
| physiological function | arginyltransferase 1 (Ate1) mediates protein arginylation, a protein posttranslational modification (PTM) in eukaryotic cells. Ate1 is required to suppress mutation frequency in yeast and mammalian cells during DNA-damaging conditions such as ultraviolet irradiation. Ate1 and arginylation are upregulated during stress and are responsible for cell death, role of Ate1/arginylation in stress response, overview. Ate1 is essential for the suppression of mutagenesis during DNA-damaging stress. Growth arrest and cell death during stress could be interpreted as a mechanism to prevent incorporation of damaged genetic material or transmission of mutation to the subsequent generations | Homo sapiens |
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