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Information on EC 6.1.1.1 - tyrosine-tRNA ligase and Organism(s) Homo sapiens and UniProt Accession Q9Y2Z4
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6.1.1.1 tyrosine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.1
- synthetases
- aminoacylation
-
tyrosylation
- stearothermophilus
-
anticodon
-
amber
- jannaschii
- trprs
-
aarss
- methanococcus
-
kmsks
-
tryptophanyl-trna
-
charcot-marie-tooth
-
mischarging
-
trna-like
- d-tyrosine
-
self-splicing
- methanocaldococcus
-
half-of-the-sites
- elr
-
non-cognate
- methionyl-trna
-
isoleucyl-trna
- medicine
- biotechnology
-
sideroblastic
-
anticodon-binding
-
tyrts
- 3-iodo-l-tyrosine
- glycyl-trna
- drug development
- pharmacology
- leurs
-
misacylation
- phenylalanyl-trna
-
fersht
-
brome
- hisrs
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
tyrosyl-trna synthetase, tyrrs, cyt-18, mitochondrial tyrosyl-trna synthetase, mini-tyrrs, tyrrss, cyt-18 protein, tyrosyl trna synthetase, mttyrrs, ldtyrrs, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Tyrosine translase
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-
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Tyrosine tRNA synthetase
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-
-
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Tyrosine--tRNA ligase
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-
-
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Tyrosine-transfer ribonucleate synthetase
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-
-
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Tyrosine-transfer RNA ligase
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-
-
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Tyrosyl--tRNA ligase
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-
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Tyrosyl-transfer ribonucleate synthetase
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-
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Tyrosyl-transfer ribonucleic acid synthetase
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Tyrosyl-transfer RNA synthetase
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Tyrosyl-tRNA ligase
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Tyrosyl-tRNA synthetase
TyrRS
Tyrosyl-tRNA synthetase
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-
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Tyrosyl-tRNA synthetase
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TyrRS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
S224 and S226 are involved in the catalytic mechanism, the sequence 222KKSSS226, termed KMSSS motif, stabilizes the the transition state for the tyrosine activation reactionby interacting with the diphosphate moiety of ATP
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ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
functional importance of Ser200 in the catalytic domain in line with an involvement of A73 rather than N1-N72 in tyrosine identity, active site structure, role of clusters 1 and 2 in tRNATyr acceptor arm
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Acylation
esterification
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-
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Acylation
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SYSTEMATIC NAME
IUBMB Comments
L-tyrosine:tRNATyr ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9023-45-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
the enzyme aminoacylates Escherichia coli tRNA as well as in vitro transcribed human mitochondrial tRNAs
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
2-step reaction mechanism, 1. activation of the amino acid by MgATP2- to form an enzyme-bound aminoacyl-adenylate intermediate, 2. transfer of the amino acid to the 3'-end of its cognate tRNATyr
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r
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
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2-step reaction, 1. activation of L-tyrosine with ATP to form L-Tyr-AMP, 2. transfer of the tyrosyl-group to tRNATyr
-
?
additional information
?
-
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the enzyme's C-terminal domain, an EMAP II-like protein, is active in angiogenesis pathways and stimulates immune cells, when cleaved off the enzyme, it stimulates blood vessel development
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?
additional information
?
-
-
TyrRS deficiency is involved in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, overview
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-
?
additional information
?
-
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recombinant hTyrRS also synthesizes kyotorphin from tyrosine, arginine, and ATP, cf. EC 6.3.2.24
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
additional information
?
-
-
the enzyme's C-terminal domain, an EMAP II-like protein, is active in angiogenesis pathways and stimulates immune cells, when cleaved off the enzyme, it stimulates blood vessel development
-
?
additional information
?
-
-
TyrRS deficiency is involved in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
K+
-
activates the wild-type enzyme and mutants S225A and K231A, no interaction with the KMSSS motif
K+
-
dependent on, required for catalysis of the tyrosine activation step, 260fold increase of the froward reaction constant
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
fluorescence emission measurement for determination of steady-state kinetics for the His-tagged and the non-His-tagged recombinant enzyme
-
additional information
additional information
-
the C-terminal His-tag of the recombinant enzyme has little effect on the catalytic activity
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the C-terminal His-tag of the recombinant enzyme has little effect on the catalytic activity
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
in vitro tyrosylation efficiency is decreased 600fold for mutant A22G (mitochondrial gene mutation T5874C), 40fold for G15A (C5877T), and is without significant effect on U54C (A5843G)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
differentiating, YARS locates mostly in the granular structures of the growth cone, branch points and the most distal part of of projecting neurites, co-localization with synaptophysin
additional information
-
YARS is expressed ubiquitously, in neuronal cells making extensions, the enzyme is located at outgrowth behaving like an early polarity maker, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
human mitochondrial and cytosolic enzymes are encoded by two different sets of genes
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axonal termini in differentiating primary motor neuron and neuroblastoma cultures
additional information
-
the mt-TyrRS is strictly mitochondrial, mitochondrial idiosyncrasies
additional information
-
the C-terminal EMAP II-like protein domain of the enzyme is probably responsible for mediation of enzyme export
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additional information
-
subcellular localization of wild-type and mutant YARS, overview
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
-
dissociating quaternary structures regulating novel functions of other tRNA synthetases
physiological function
-
although native TyrRS has no known cytokine functions, natural proteolysis of secreted TyrRS releases TyrRSMini, which not only has the same aminoacylation activity as native TyrRS when occuring as a dimer, the monomer is inactive, but TyrRSMini also has strong activity for stimulating migration of polymorphonuclear leukocytes. The migration-stimulating activity is dependent on an ELR tripeptide motif, similar to that in CXC cytokines like IL-8, and also has the familiar bell-shaped concentration dependence seen for CXC cytokines. But TyrRSMini does not induce internalization of CXCR1/2. The TyrRSMini monomer is an agonist, while TyrRSMini dimer is an antagonist of induced PMN cell migration
physiological function
-
the human TyrRS can be split into two fragments with distinct signaling activities. The N-terminal fragment is an IL-8-like cytokine whereas the C-terminal fragment is more similar to endothelial monocyte-activating polypeptide II (EMAP II). Therapeutic effect of recombinant human tyrosyl-tRNA synthetase (rhTyrRS) against development of thrombocytopenia in cyclophosphamide (CTX) treated mice. Recombinant hTyrRS promotes migration and aggregation of megakaryocytes to the bone marrow niche. 1 is particularly important for the adhesion. The N-terminal fragment of the recombinant TyrRS acts as a chemoattractant molecule for M-07e cells, it stimulates adhesion of THP-1 cells to HUVECs and plays a role in the transendothelial migration of megakaryocytes and thrombocytopoiesis. All mice pretreated with rhTyrRS show a dose-dependent increase in megakaryocytes localized to the sinusoids. Recombinant human TyrRS enhances survival of cyclophosphamide (CTX) treated mice, that the bone marrow endothelial cells may enhance survival of megakaryocytes in the presence of rhTyrRS pretreatment
physiological function
-
tyrosyl-tRNA synthetase is a potential kyotorphin synthetase (i.e. tyrosine-arginine ligase, EC 6.3.2.24) in mammals
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SYYM_HUMAN
477
0
53199
Swiss-Prot
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
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homodimeric mitochondrial enzyme crystal structure analysis, the active mutant mitochondrial enzyme, deprived of the C-terminal S4-like domain, resembles eubacterial TyrRSs with a canonical tyrosine-binding pocket and adenylate-binding residues typical of class I synthetases, mt-TyrRS shows an asymmetry propagating from the dimer interface toward the two catalytic sites and extremities of each subunit, structure comparisons with other TyrRSs, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the C-terminal domain of the enzyme, which has cytokine and angiogenic activity and stimulates immune cells, is isolated by proteolytic cleavage or alternative splicing, the mini enzyme is a stimulator of blood vessel development, the full-length enzyme is inactive
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant mt-TyrRS-DS4, lacking the C-terminal S4-like domain, in complex with Tyr-AMS, an adenylate analogue, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E196K
-
naturally occuring mutation in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, the mutant enzyme shows reduced activity and specific distribution in the cell compared to the wild-type enzyme, no functional complementation of a Saccharomyces cerevisiae TYS1 mutant strain, the mutant shows altered distribution in neuronal cells compared to the wild-type enzyme when recombinantly expressed
G41R
-
naturally occuring mutation in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, the mutant enzyme shows reduced activity and specific distribution in the cell compared to the wild-type enzyme, partial functional complementation of a Saccharomyces cerevisiae TYS1 mutant strain, the mutant shows altered distribution in neuronal cells compared to the wild-type enzyme when recombinantly expressed
K231A
-
site-directed mutagenesis, no effect on the catalytic activity of the enzyme
M252A
-
site-directed mutagenesis, the mutant is fully active in ATP/diphosphate exchange, indicating that the site for tyrosyl-adenylate formation remains unperturbed upon mutation, tRNA mutant U73 is no more charged by mt-TyrRS upon Met252Ala mutation, the weak tyrosylation activity of tRNATyr with G73 is completely abolished, mutating Met252 shows only faint effects on wild-type and mutants mt-tRNATyr charging as compared to the wild-type enzyme
mini-TyrRS_TyrRS(ELQ)
the surface helix encodes an ELR motif that functions like the ELR tripeptide in CXC cytokines, substitution of Arg93 to generate ELQ
mini-TyrRS_TyrRS(EYR)
the surface helix encodes an ELR motif that functions like the ELR tripeptide in CXC cytokines, substitution of Leu92 to generate EYR
mini-TyrRS_TyrRS(NLR)
the surface helix encodes an ELR motif that functions like the ELR tripeptide in CXC cytokines, substitution of Glu91 to generate NLR
Q202A
-
site-directed mutagenesis, the mutant is fully active in ATP/diphosphate exchange, indicating that the site for tyrosyl-adenylate formation remains unperturbed upon mutation, the weak tyrosylation activity of tRNATyr with G73 is completely abolished, mutating Gln202 shows only faint effects on wild-type and mutants mt-tRNATyr charging as compared to the wild-type enzyme
S200A
-
site-directed mutagenesis, the mutant is fully active in ATP/diphosphate exchange, indicating that the site for tyrosyl-adenylate formation remains unperturbed upon mutation, replacing Ser200 with Glu completely abolishes tyrosylation activity of wild-type and mutated tRNATyr transcripts
S224A
-
site-directed mutagenesis, 7.5fold decrease of the forward rate constant
S225A
-
site-directed mutagenesis, no effect on the catalytic activity of the enzyme
TyrRS_153-156delVKQV
-
dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
TyrRS_E196K
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dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
TyrRS_G41R
-
dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
additional information
additional information
-
disrupted function and axonal distribution of the mutant enzyme in autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C, a common disorder of the peripheral nervous system, caused by demyelination or axonal degeneration or a combination of both, mutant families analysis, mutation analysis, phenotype, overview
additional information
two closely related, internally deleted, splice variants of homodimeric human tyrosyl-tRNA synthetase (TyrRS) are analyzed, in spite of both variants ablating a portion of the catalytic core and dimer-interface contacts of native TyrRS, each folded into a distinct stable structure. The internal deletion of TyrRSE2-4 splice variant gives an alternative, neomorphic dimer interface orthogonal to that of native TyrRS. One splice variant, TyrRSE2-4, is largely dimeric while the other is mostly monomeric. TyrRS SVs are specifically enriched in lymphocytes and lung tissue
additional information
-
two closely related, internally deleted, splice variants of homodimeric human tyrosyl-tRNA synthetase (TyrRS) are analyzed, in spite of both variants ablating a portion of the catalytic core and dimer-interface contacts of native TyrRS, each folded into a distinct stable structure. The internal deletion of TyrRSE2-4 splice variant gives an alternative, neomorphic dimer interface orthogonal to that of native TyrRS. One splice variant, TyrRSE2-4, is largely dimeric while the other is mostly monomeric. TyrRS SVs are specifically enriched in lymphocytes and lung tissue
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by utilizing the His-tag
recombinant His-Tagged enzyme form Escherichia coli strain BL21(DE3), removal of the N-terminal His-tag
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recombinant His-tagged full-length wild-type and mutant mitochondrial enzymes, and truncated mutant mt-TyrRS-DS4 mitochondrial enzyme from Escherichia coli by nickel affinity chromatography
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recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant thioredoxin-His-tagged enzyme splice variants from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination of wild-type and mutant enzymes, localization of the gene encoding the enzyme on chromosome 1p34-p35, functional complementation of a Saccharomyces cerevisiae TYS1 mutant strain, overview, transient expression of EGFP-tagged wild-type and mutant enzymes in murine neuroblastoma N2a cells
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expression of His-tagged full-length wild-type and truncated mutant enzymes in Escherichia coli
-
expression of the enzyme as His-tagged protein in Escherichia coli strain BL21(DE3)
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expression of wild-type and mutant enzymes as His-tagged proteins in Escherichia coli
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gene TyrS, DNA sequence determination, overexpression as His-tagged enzyme in Escherichia coli BL21
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mutant human mini-TyrRS constructs are generated using QuikChange site-directed mutagenesis kit and using a plasmid encoding the gene for wild-type human mini-TyrRS as the template for PCR mutagenesis reactions, all proteins are expressed with a C-terminal His-tag to facilitate purification
recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
tyrS, DNA and amino acid sequence determination and analysis, analysis of two closely related, internally deleted, splice variants of homodimeric human tyrosyl-tRNA synthetase (TyrRS). Detection of the TyrRS transcripts in the cytoplasmic and polyribosomal RNA is carried out by PCR using primers targeting the 5'-UTR/exon1 and exon5/exon6 regions of the TyrRS gene (FP and RP2). Recombinant expression of splice variants in Jurkat T, THP-1, or HEK-293T cells, and recombinant expression of splice variants as thioredoxin-His-tagged proteins in Escherichia coli strain BL21(DE3), removal of the tag by protease-3C, followed by gel filtration
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
pharmacology
-
design of antimicrobials that target the bacterial enzyme of Bacillus stearothermophilus making use of the differences between the actives sites of the 2 enzymes
medicine
-
dominant-intermediate Charcot-Marie-Tooth neuropathy, DI-CMT, is characterized by axonal degeneration and demyelination of peripheral motor and sensory neurons, three dominant mutations in the YARS gene, encoding tyrosyl-tRNA synthetase, have so far been associated with DI-CMT type C
medicine
some mammalian synthetases develop cytokine functions possibly linked to disease-causing mutations in tRNA synthetases
medicine
-
recombinant hTyrRS might be a useful therapeutic agent for chemotherapy-induced thrombocytopenia. Intraperitoneal administration of at least 0.01 mg/day recombinant hTyrRS for 7 days significantly prevents the decrease in platelets 8 days after cyclophosphamide injection
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ewalt, K.L.; Schimmel, P.
Activation of angiogenic signaling pathways by two human tRNA synthetases
Biochemistry
41
13344-13349
2002
Homo sapiens
Austin, J.; First, E.A.
Catalysis of tyrosyl-adenylate formation by the human tyrosyl-tRNA synthetase
J. Biol. Chem.
277
14812-14820
2002
Homo sapiens
Austin, J.; First, E.A.
Comparison of the catalytic roles played by the KMSKS motif in the human and Bacillus stearothermophilus trosyl-tRNA synthetases
J. Biol. Chem.
277
28394-28399
2002
Geobacillus stearothermophilus, Homo sapiens
Jia, J.; Li, B.; Jin, Y.; Wang, D.
Expression, purification, and characterization of human tyrosyl-tRNA synthetase
Protein Expr. Purif.
27
104-108
2003
Homo sapiens
Bonnefond, L.; Fender, A.; Rudinger-Thirion, J.; Giege, R.; Florentz, C.; Sissler, M.
Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS
Biochemistry
44
4805-4816
2005
Homo sapiens (Q9Y2Z4), Homo sapiens
Jordanova, A.; Irobi, J.; Thomas, F.P.; Van Dijck, P.; Meerschaert, K.; Dewil, M.; Dierick, I.; Jacobs, A.; De Vriendt, E.; Guergueltcheva, V.; Rao, C.V.; Tournev, I.; Gondim, F.A.; DHooghe, M.; Van Gerwen, V.; Callaerts, P.; Van Den Bosch, L.; Timmermans, J.P.; Robberecht, W.; Gettemans, J.; The, T.h.e.v.
Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy
Nat. Genet.
38
197-202
2006
Homo sapiens
Bonnefond, L.; Frugier, M.; Touze, E.; Lorber, B.; Florentz, C.; Giege, R.; Sauter, C.; Rudinger-Thirion, J.
Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features
Structure
15
1505-1516
2007
Homo sapiens
Bonnefond, L.; Florentz, C.; Giege, R.; Rudinger-Thirion, J.
Decreased aminoacylation in pathology-related mutants of mitochondrial tRNATyr is associated with structural perturbations in tRNA architecture
RNA
14
641-648
2008
Homo sapiens
Kapoor, M.; Otero, F.J.; Slike, B.M.; Ewalt, K.L.; Yang, X.L.
Mutational separation of aminoacylation and cytokine activities of human tyrosyl-tRNA synthetase
Chem. Biol.
16
531-539
2009
Homo sapiens (P54577), Homo sapiens
Storkebaum, E.; Leitao-Goncalves, R.; Godenschwege, T.; Nangle, L.; Mejia, M.; Bosmans, I.; Ooms, T.; Jacobs, A.; Van Dijck, P.; Yang, X.L.; Schimmel, P.; Norga, K.; Timmerman, V.; Callaerts, P.; Jordanova, A.
Dominant mutations in the tyrosyl-tRNA synthetase gene recapitulate in Drosophila features of human Charcot-Marie-Tooth neuropathy
Proc. Natl. Acad. Sci. USA
106
11782-11787
2009
Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens
Vo, M.N.; Yang, X.L.; Schimmel, P.
Dissociating quaternary structure regulates cell-signaling functions of a secreted human tRNA synthetase
J. Biol. Chem.
286
11563-11568
2011
Homo sapiens
Savytskyi, O.V.; Yesylevskyy, S.O.; Kornelyuk, A.I.
Asymmetric structure and domain binding interfaces of human tyrosyl-tRNA synthetase studied by molecular dynamics simulations
J. Mol. Recognit.
26
113-120
2013
Homo sapiens (P54577), Homo sapiens
Ling, Z.; Yanling, Z.; Zhe, F.; Kui, C.; Xiushi, Z.; Min, Y.; Wei, M.
Recombinant human tyrosyl-tRNA synthetase, a novel thrombopoietic agent
Eur. J. Pharmacol.
738
293-300
2014
Homo sapiens
Wei, Z.; Xu, Z.; Liu, X.; Lo, W.S.; Ye, F.; Lau, C.F.; Wang, F.; Zhou, J.J.; Nangle, L.A.; Yang, X.L.; Zhang, M.; Schimmel, P.
Alternative splicing creates two new architectures for human tyrosyl-tRNA synthetase
Nucleic Acids Res.
44
1247-1255
2016
Homo sapiens (P54577), Homo sapiens
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