Literature summary for 2.3.2.8 extracted from

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

Cloned(Commentary)

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Source Tissue

Source Tissue	Comment	Organism	Textmining
meristem	-	Physcomitrium patens	-
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)

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

Subunits	Comment	Organism
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
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
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
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
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
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
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

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

General Information

General Information	Comment	Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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