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Arginyltransferase 1

ATE1, R-transferase, arginyltransferase, arginyl-tRNA-protein transferase
This gene encodes an arginyltransferase, an enzyme that is involved in posttranslational conjugation of arginine to N-terminal aspartate or glutamate residues. Conjugation of arginine to the N-terminal aspartate or glutamate targets proteins for ubiquitin-dependent degradation. Alternative splicing results in two transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, Ubiquitin, ACID, HAD, Actin
Papers on ATE1
Reduced passive force in skeletal muscles lacking protein arginylation.
Rassier et al., Montréal, Canada. In Am J Physiol Cell Physiol, Feb 2016
Key points are as follows: 1) active and passive forces were decreased in myofibrils and single sarcomeres isolated from muscles lacking arginyl-tRNA-protein transferase (ATE1).
Arginyltransferase suppresses cell tumorigenic potential and inversely correlates with metastases in human cancers.
Kashina et al., Philadelphia, United States. In Oncogene, Jan 2016
UNASSIGNED: Arginylation is an emerging post-translational modification mediated by arginyltransferase (ATE1) that is essential for mammalian embryogenesis and regulation of the cytoskeleton.
Amino-terminal arginylation as a degradation signal for selective autophagy.
Kim et al., South Korea. In Bmb Rep, Sep 2015
We showed that many ER residents, such as BiP, contain evolutionally conserved arginylation permissive pro-N-degrons, and that certain inducers like dsDNA or proteasome inhibitors cause their translocation into the cytoplasm where they bind misfolded proteins and undergo amino-terminal arginylation by arginyl transferase 1 (ATE1).
Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding.
Kwon et al., South Korea. In Nat Cell Biol, Jul 2015
We show that ATE1-encoded Arg-transfer RNA transferase (R-transferase) of the N-end rule pathway mediates N-terminal arginylation of multiple endoplasmic reticulum (ER)-residing chaperones, leading to their cytosolic relocalization and turnover.
Assaying ATE1 Activity In Vitro.
Kashina et al., Philadelphia, United States. In Methods Mol Biol, 2014
Here we describe a standard arginyltransferase assay in vitro using bacterially expressed purified ATE1 in a system with minimal number of components (Arg, tRNA, Arg-tRNA synthetase, and arginylation substrate).
Bacterial Expression and Purification of Recombinant Arginyltransferase (ATE1) and Arg-tRNA Synthetase (RRS) for Arginylation Assays.
Kashina et al., Philadelphia, United States. In Methods Mol Biol, 2014
Here we describe the procedure for expression and purification of recombinant ATE1 from E. coli.
Arginyltransferase: A Personal and Historical Perspective.
Soffer, New York City, United States. In Methods Mol Biol, 2014
In the late 1960s and early 1970s, characterization of arginylation has been spearheaded via biochemical studies that enabled the first characterization of ATE1 and its substrate specificity.
Applying Arginylation for Bottom-Up Proteomics.
Ebhardt, Zürich, Switzerland. In Methods Mol Biol, 2014
Arginylation is an enzymatic reaction in which arginyl-tRNA protein transferase 1 (ATE1, EC conjugates a single arginyl moiety from aminoacylated tRNA(Arg) onto a target polypeptide.
Transferase-Mediated Labeling of Protein N-Termini with Click Chemistry Handles.
Petersson et al., Philadelphia, United States. In Methods Mol Biol, 2014
This method can be used to directly detect AaT substrates or in a two-step protocol to detect substrates of the mammalian ATE1 transferase.
Assay of Arginyltransferase Activity by a Fluorescent HPLC Method.
Takao, Sakado, Japan. In Methods Mol Biol, 2014
Syntheses of fluorescent substrate and product for arginyltransferase, N-aspartyl-N'-dansylamido-1,4-butanediamine (Asp-4DNS), and N-arginylaspartyl-N'-dansylamido-1,4-butanediamine (ArgAsp-4DNS), respectively, including their precursor 4-dansylamidobutylamine (4DNS), are described.
High-Throughput Arginylation Assay in Microplate Format.
Kashina et al., Tezpur, India. In Methods Mol Biol, 2014
Here we describe the biochemical assay for ATE1-mediated arginylation in microplate format, which can be applied to high-throughput screens for identification of small-molecule inhibitors and activators of ATE1, high-volume analysis of ATE1 substrates, and other similar applications.
Protein arginylation, a global biological regulator that targets actin cytoskeleton and the muscle.
Kashina, Philadelphia, United States. In Anat Rec (hoboken), 2014
Posttranslational addition of Arg to proteins, mediated by arginyltransferase ATE1 has been first observed in 1963 and remained poorly understood for decades since its original discovery.
Characterization of arginylation branch of N-end rule pathway in G-protein-mediated proliferation and signaling of cardiomyocytes.
Kwon et al., South Korea. In J Biol Chem, 2012
Data indicate that arginyl-tRNA-protein transferase ATE1-deficient myocardium and cardiomyocytes showed reduced DNA synthesis and mitotic activity.
Posttranslational arginylation as a global biological regulator.
Kashina et al., Philadelphia, United States. In Dev Biol, 2011
Among such modifications, an important role belongs to protein arginylation - posttranslational tRNA-mediated addition of arginine, to proteins by arginyltransferase, ATE1.
Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo.
Kashina et al., Philadelphia, United States. In Chem Biol, 2011
ATE1 function and molecular requirements
The arginylation-dependent association of calreticulin with stress granules is regulated by calcium.
Hallak et al., Córdoba, Argentina. In Biochem J, 2010
Cytoplasmic calreticulin is arginylated by ATE1.
Arginyltransferase regulates alpha cardiac actin function, myofibril formation and contractility during heart development.
Kashina et al., Philadelphia, United States. In Development, 2008
The role of arginylation in the development and function of cardiac myocytes and their actin-containing structures during embryogenesis, was investigated.
Conditional Tek promoter-driven deletion of arginyltransferase in the germ line causes defects in gametogenesis and early embryonic lethality in mice.
Kashina et al., Philadelphia, United States. In Plos One, 2008
analysis of a defect in gametogenesis originating from Tek-driven Ate1 deletion in premeiotic germ cells
The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators.
Varshavsky et al., Pasadena, United States. In Nature, 2005
oxidation of N-terminal cysteine is essential for its arginylation; levels of regulatory proteins bearing N-terminal cysteine, such as RGS4, RGS5 and RGS16, are greatly increased in mouse ATE1-/- embryos, which lack arginylation
An essential role of N-terminal arginylation in cardiovascular development.
Varshavsky et al., Pasadena, United States. In Science, 2002
role in cardiovascular development
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