Cloned (Comment) | Organism |
---|---|
gene PHYPA_004926, single copy gene, phylogenetic analysis | Physcomitrium patens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | ATE abundance underlies spatiotemporal patterning in the moss Physcomitrella patens using a translational GUS reporter fusion via knock-in at the endogenous genomic locus. The tagged version of ATE is used to pull down specifically ATE together with potential interaction partners from tissues where ATE abundance is monitored via histochemical GUS staining | Physcomitrium patens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginyl-tRNAArg + protein | Physcomitrium patens | - |
tRNAArg + L-arginyl-[protein] | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Physcomitrium patens | A0A2K1KVV8 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
gametophore | young | Physcomitrium patens | - |
meristem | - |
Physcomitrium patens | - |
shoot | - |
Physcomitrium patens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginyl-tRNAArg + protein | - |
Physcomitrium patens | tRNAArg + L-arginyl-[protein] | - |
? | |
additional information | the enzyme interacts with sHSP17.2a, an Hsp20 class I chaperone | Physcomitrium patens | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
arginyl-tRNA protein transferase | - |
Physcomitrium patens |
ATE | - |
Physcomitrium patens |
Organism | Comment | Expression |
---|---|---|
Physcomitrium patens | ATE abundance is increased in moss (Physcomitrella patens) leafy gametophores after application of the stress hormone abscisic acid (ABA), in darkness or in red light, using a translational ATE:GUS fusion at the endogenous locus | up |
General Information | Comment | Organism |
---|---|---|
additional information | identification of targets and interaction partners, e.g. sHSP17.2a chaperone, of arginyl-tRNA protein transferase (ATE) in the model plant Physcomitrella patens by mass spectrometry, employing two different immunoaffinity strategies and a recently established transgenic ATE:GUS reporter line. A commercially available antibody against the fused reporter protein (beta-glucuronidase) to pull down ATE and its interacting proteins. Preparation of specific antibodies and immunoprecipitation of arginylated proteins, overview. Arginylated peptides are reliably identified for three different proteins namely acylamino-acid releasing enzyme (PpAARE, Pp1s619_3V6.1), an uncharacterized protein (UP, Pp1s68_62V6.1) and a putative AAA-type ATPase (PpATAD3.1, Pp1s106_174V6.1), and for one additional protein, an ABC transporter family protein (PpABCB20, Pp1s29_108V6.1). The identified arginylation do not represent a side-chain arginylation as the a1 ion of a dimethylated arginine is present in the corresponding HCD spectrum | Physcomitrium patens |
physiological function | arginyltransferases (ATE) mediates N-terminal arginylation of secondary destabilizing residues (D, E, Cox) | Physcomitrium patens |