Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Domitrovic, T.; Fausto, A.; Silva, T.; Romanel, E.; Vaslin, M.
    Plant arginyltransferases (ATEs) (2017), Genet. Mol. Biol., 40, 253-260 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.8 gene ATE1 or At5g05700, sequence comparisons, phylogenetic analysis and domain location of ATE protein sequences among plant species Arabidopsis thaliana
2.3.2.8 gene ATE1_1, phylogenetic analysis and domain location of ATE protein sequences among plant species Vitis vinifera
2.3.2.8 gene CHLRE_13g580600v5, phylogenetic analysis and domain location of ATE protein sequences among plant species Chlamydomonas reinhardtii
2.3.2.8 gene Os05g0446800, phylogenetic analysis and domain location of ATE protein sequences among plant species Oryza sativa Japonica Group
2.3.2.8 gene PHYPA_004926, phylogenetic analysis and domain location of ATE protein sequences among plant species Physcomitrium patens
2.3.2.8 gene POPTR_010G190100, phylogenetic analysis and domain location of ATE protein sequences among plant species Populus trichocarpa
2.3.2.8 gene SORBI_3009G156000, phylogenetic analysis and domain location of ATE protein sequences among plant species Sorghum bicolor

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.8 L-arginyl-tRNAArg + protein Arabidopsis thaliana
-
 tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein Physcomitrium patens
-
 tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein Chlamydomonas reinhardtii
-
 tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein Populus trichocarpa
-
 tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein Sorghum bicolor
-
 tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein Vitis vinifera
-
 tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein Oryza sativa Japonica Group
-
 tRNAArg + L-arginyl-[protein]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.8 Arabidopsis thaliana Q9ZT48
-
-
2.3.2.8 Chlamydomonas reinhardtii A0A2K3D0B7
-
-
2.3.2.8 Oryza sativa Japonica Group Q688J5
-
-
2.3.2.8 Physcomitrium patens A0A2K1KVV8
-
-
2.3.2.8 Populus trichocarpa A0A2K1YWL5
-
-
2.3.2.8 Sorghum bicolor C5YYU0
-
-
2.3.2.8 Vitis vinifera A0A438HA55
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.8 meristem
-
 Physcomitrium patens
-
2.3.2.8 additional information ATE protein abundance is spatially and temporally regulated by hormones and light and is highly abundant in meristematic cells Physcomitrium patens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.8 L-arginyl-tRNAArg + EBP Pseudomonas syringae ethylene response factor 72 (EBP) is a putative substrate for ATE1 Arabidopsis thaliana tRNAArg + L-arginyl-[EBP]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein
-
 Arabidopsis thaliana tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein
-
 Physcomitrium patens tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein
-
 Chlamydomonas reinhardtii tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein
-
 Populus trichocarpa tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein
-
 Sorghum bicolor tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein
-
 Vitis vinifera tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + protein
-
 Oryza sativa Japonica Group tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + RIN4 Pseudomonas syringae 1-interacting protein 4 (RIN4) is a putative substrate for ATE1 Arabidopsis thaliana tRNAArg + L-arginyl-[RIN4]
-
 ?
2.3.2.8 L-arginyl-tRNAArg + VRN2 Pseudomonas syringae vernalization 2 protein (VRN2) is a putative substrate for ATE1 Arabidopsis thaliana tRNAArg + L-arginyl-[VRN2]
-
 ?
2.3.2.8 additional information N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates Physcomitrium patens ?
-
-
2.3.2.8 additional information N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates Chlamydomonas reinhardtii ?
-
-
2.3.2.8 additional information N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates Populus trichocarpa ?
-
-
2.3.2.8 additional information N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates Sorghum bicolor ?
-
-
2.3.2.8 additional information N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates Vitis vinifera ?
-
-
2.3.2.8 additional information N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates Oryza sativa Japonica Group ?
-
-
2.3.2.8 additional information putative substrates of ATE are identified among Nt Met-Cys proteins. N-terminal Asp, Glu, or oxidized Cys on peptides and proteins are ATE substrates Arabidopsis thaliana ?
-
-

Subunits

EC Number Subunits Comment Organism
2.3.2.8 More ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Arabidopsis thaliana
2.3.2.8 More ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Physcomitrium patens
2.3.2.8 More ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Chlamydomonas reinhardtii
2.3.2.8 More ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Populus trichocarpa
2.3.2.8 More ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Sorghum bicolor
2.3.2.8 More ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Vitis vinifera
2.3.2.8 More ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Oryza sativa Japonica Group

Synonyms

EC Number Synonyms Comment Organism
2.3.2.8 arginyl-tRNA--protein transferase UniProt Arabidopsis thaliana
2.3.2.8 arginyl-tRNA--protein transferase UniProt Chlamydomonas reinhardtii
2.3.2.8 arginyl-tRNA--protein transferase UniProt Populus trichocarpa
2.3.2.8 arginyl-tRNA--protein transferase UniProt Sorghum bicolor
2.3.2.8 arginyl-tRNA--protein transferase UniProt Vitis vinifera
2.3.2.8 arginyl-tRNA--protein transferase UniProt Oryza sativa Japonica Group
2.3.2.8 arginyl-tRNA-protein transferase UniProt Physcomitrium patens
2.3.2.8 ATE
-
 Arabidopsis thaliana
2.3.2.8 ATE
-
 Physcomitrium patens
2.3.2.8 ATE
-
 Chlamydomonas reinhardtii
2.3.2.8 ATE
-
 Populus trichocarpa
2.3.2.8 ATE
-
 Sorghum bicolor
2.3.2.8 ATE
-
 Vitis vinifera
2.3.2.8 ATE
-
 Oryza sativa Japonica Group
2.3.2.8 Ate1
-
 Arabidopsis thaliana
2.3.2.8 Ate1
-
 Physcomitrium patens
2.3.2.8 Ate1
-
 Chlamydomonas reinhardtii
2.3.2.8 Ate1
-
 Populus trichocarpa
2.3.2.8 Ate1
-
 Sorghum bicolor
2.3.2.8 Ate1
-
 Vitis vinifera
2.3.2.8 Ate1
-
 Oryza sativa Japonica Group

General Information

EC Number General Information Comment Organism
2.3.2.8 evolution plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication Arabidopsis thaliana
2.3.2.8 evolution plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication Physcomitrium patens
2.3.2.8 evolution plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication Chlamydomonas reinhardtii
2.3.2.8 evolution plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication Populus trichocarpa
2.3.2.8 evolution plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication Sorghum bicolor
2.3.2.8 evolution plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication Vitis vinifera
2.3.2.8 evolution plant ATEs and their evolutionary relationship with other ATEs, overview. Identification of two Arabidopsis thaliana Nt-amidases mediating recognition of tertiary destabilizing Nt-amino acids Asn and Gln have shown that the N-end rule pathway in plants is very similar to that in animals, highlighting a possible evolutionary common origin. But the steps related to protein degradation likely evolved after plant and animal divergence, as suggested by the differences in PRTs and UBR N-recognins. Plant evolutionary analysis has identified ATE orthologous genes from the green alga Chlamydomonas reinhardtii to angiosperms. In general, only one ATE gene is detected in a given plant species, with the two conserved ATE domains located at the N- and C-termini. Some species, such as Arabidopsis, Populus, and Sorghum, have experienced gene duplication Oryza sativa Japonica Group
2.3.2.8 malfunction the relative abundance of methylesterase 10 (MES10), nucleoside diphosphate kinase family protein (NDPK1), and two asparagine synthetases (ASNs) is augmented in ate1/ate2 mutants. Disrupted ATE1 in dls1 mutants shows an extremely slow age-dependent, dark-induced leaf senescence, phenotype. Double mutant for AtATE1 and AtATE2 (ate1.ate2) displays lost sensitivity to hormone abscisic acid and consequently uncontrolled seed germination and establishment. Arabidopsis ate1/ate2 or prt6 mutants cannot degrade ERFVII, and as a consequence show increased expression of hypoxia-responsive genes involved in fermentation and sugar consumption even under oxygen-rich conditions Arabidopsis thaliana
2.3.2.8 metabolism regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII) Physcomitrium patens
2.3.2.8 metabolism regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII) Chlamydomonas reinhardtii
2.3.2.8 metabolism regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII) Populus trichocarpa
2.3.2.8 metabolism regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII) Sorghum bicolor
2.3.2.8 metabolism regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII) Vitis vinifera
2.3.2.8 metabolism regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII) Oryza sativa Japonica Group
2.3.2.8 metabolism regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. Great importance of the ATE/N-end rule pathway in regulating plant signaling. Plant development, seed germination, leaf morphology and responses to gas signaling in plants are among the processes affected by the ATE/N-end rule pathway. The N-recognin E3 ligase PRT6 and AtATE1 and AtATE2 are involved in seed germination controlled by abscisic acid. A signaling pathways in plants controlled by arginylation is that involving the ethylene responsive transcription factor VII (ERFVII) Arabidopsis thaliana
2.3.2.8 additional information ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Arabidopsis thaliana
2.3.2.8 additional information ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Physcomitrium patens
2.3.2.8 additional information ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Chlamydomonas reinhardtii
2.3.2.8 additional information ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Populus trichocarpa
2.3.2.8 additional information ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Sorghum bicolor
2.3.2.8 additional information ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Vitis vinifera
2.3.2.8 additional information ATE protein sequences contain two Pfam domains named ATE-N (PF04376) and ATE-C (PF04377), which are located at N- and C-termini, respectively Oryza sativa Japonica Group
2.3.2.8 physiological function regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation Physcomitrium patens
2.3.2.8 physiological function regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation Vitis vinifera
2.3.2.8 physiological function regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation Oryza sativa Japonica Group
2.3.2.8 physiological function regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation. In plants, ATE is not required for viability Chlamydomonas reinhardtii
2.3.2.8 physiological function regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation. In plants, ATE is not required for viability Populus trichocarpa
2.3.2.8 physiological function regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation. In plants, ATE is not required for viability Sorghum bicolor
2.3.2.8 physiological function regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes, proposed model of biological processes regulated by ATE arginylation in plants, overview. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. Biological functions of plant ATE proteins, overview. Asp, Glu, or oxidized Cys are ATE substrates, and the protein may become a substrate for E3 ligases following arginylation. In plants, ATE is not required for viability. The arginylation branch of the N-end rule pathway is also responsible for repressing expression of the meristempromoting brevipedicellus (BP) gene during leaf development, acting in a redundant way with the asymmetric leaves 1 (AS1) transcription factor complex, a known negative regulator of BP expression Arabidopsis thaliana