The aminoacyl-tRNA synthetases (EC 6.1.1.) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices, and are mostly dimeric or multimeric, containing at least three conserved regions. However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2-hydroxyl of the tRNA, while, in class II reactions, the 3-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, ...

The tRNA content and aminoacyl-tRNA synthetases of regenerating liver in the phase of rapid growth were compared with those of livers from both intact and sham-operated rats. At 48 h after hepatectomy, the amount of active tRNA (called total acceptor capacity) is significantly higher in regenerating liver than in control livers, owing to a general, possibly not uniform, increase in the various tRNA families, which suggests that it may contribute to the increased protein synthesis and to decreased protein degradation as well. The activities of most, but not of all, aminoacyl-tRNA synthetases in cell sap of regenerating liver tend to be greater than normal. Increased activity of histidyl-tRNA synthetase fits in with the possibility that the mechanisms that control the rate of protein degradation through aminoacylation of tRNAHis in cultured cells [Scornik (1983) J. Biol. Chem. 258, 882-886] also operate in the liver and play a role in regeneration. Sedimentation analysis of cell sap in sucrose ...

Aminoacyl‐tRNA synthetases (aaRSs) comprise an ancient, diverse enzyme family that catalyzes specific attachment of amino acids to their cognate tRNAs and ensures the accurate translation of the genetic code in the first step of protein synthesis (Carter, 1993; Martinis and Schimmel, 1996). The aminoacylation reaction is accomplished by a two‐step process: (a) activation of amino acids with ATP, forming aminoacyl adenylate, and (b) transfer of the aminoacyl residue to the 3′‐end of tRNA (Ibba and Söll, 2000). In this two‐step reaction, each tRNA synthetase molecule must select and activate its cognate amino acid from the cellular pool of 20 different proteinaceous amino acids. Because of the structural similarity of some amino acids, aaRSs really have difficulties in accurately discriminating cognate substrate from others (Baldwin and Berg, 1966; Loftfield and Vanderjagt, 1972). High fidelity in the amino‐acid selection process, which in some cases depends on hydrolytic editing to ...

Aminoacyl-tRNA synthetases are a group of enzymes which activate amino acids and transfer them to specific tRNA molecules as the first step in protein biosynthesis. In prokaryotic organisms there are at least twenty different types of aminoacyl-tRNA synthetases, one for each different amino acid. In eukaryotes there are generally two aminoacyl-tRNA synthetases for each different amino acid: one cytosolic form and a mitochondrial form ...

Why do ARSs form a complex? Channeling is clearly one possibility. Channeling has been suggested as an efficient way to utilize substrate for sequential reactions (Srere, 1987). For example, for sequential metabolic enzymes, stimulation of the first enzyme induced by a protein-protein interaction with the next provides a structural basis for channeling. The supramolecular assemblies of ARSs and elongation factors (Mirande, 1991; Kisselev and Wolfson, 1994; Yang, 1996) represent structural evidence for the subcellular organization of the protein synthesis machinery. Moreover, the existence of a channeled tRNA cycle during mammalian protein synthesis provides functional evidence for cellular compartmentalization of translation (Negrutskii and Deutscher, 1991; Negrutskii et al., 1994; Stapulionis and Deutscher, 1995). According to the proposed channeling scheme, aminoacyl-tRNAs are vectorially transferred from ARSs to ribosomes as ternary complexes of EF-1α, GTP and aminoacyl-tRNA (Negrutskii and ...

wrt-10 encodes a hedgehog-like protein, with an N-terminal signal sequence, a Wart domain, and a C-terminal region of low-complexity sequence. WRT-10 is expressed in both male and hermaphrodite intestine. the Wart domain is predicted to form a cysteine-crosslinked protein involved in intercellular signalling, and it has subtle similarity to the N-terminal Hedge domain of HEDGEHOG proteins. WRT-10 is required for normal growth to full size and locomotion. both of these requirements may reflect common defects in cholesterol-dependent hedgehog-like signalling or in vesicle trafficking. [Source: WormBase]wrt-10 encodes a hedgehog-like protein, with an N-terminal signal sequence, a Wart domain, and a C-terminal region of low-complexity sequence. WRT-10 is expressed in both male and hermaphrodite intestine. the Wart domain is predicted to form a cysteine-crosslinked protein involved in intercellular signalling, and it has subtle similarity to the N-terminal Hedge domain of HEDGEHOG proteins. WRT-10 is ...

Tuberculosis, caused by Mycobacterium tuberculosis, responsible for ∼1.5 million fatalities in 2018, is the deadliest infectious disease. Global spread of multidrug resistant strains is a public health threat, requiring new treatments. Aminoacyl-tRNA synthetases are plausible candidates as potential drug targets, because they play an essential role in translating the DNA code into protein sequence by attaching a specific amino acid to their cognate tRNAs. We report structures of M. tuberculosis Phe-tRNA synthetase complexed with an unmodified tRNAPhe transcript and either L-Phe or a nonhydrolyzable phenylalanine adenylate analog. High-resolution models reveal details of two modes of tRNA interaction with the enzyme: an initial recognition via indirect readout of anticodon stem-loop and aminoacylation ready state involving interactions of the 3′ end of tRNAPhe with the adenylate site. For the first time, we observe the protein gate controlling access to the active site and detailed geometry ...

Glutamyl-tRNA synthetase of Escherichia coli. Isolation and primary structure of the gltX gene and homology with other aminoacyl-tRNA synthetases. J. Biol. Chem. 261 (23), 10610-10617 (1986 ...

Aminoacyl tRNA synthetases establish the genetic code through their aminoacylations of transfer RNAs. These universal, essential enzymes arose early in evolution, presumably taking over the role of ribozymes to establish the code. Sequence relationships b

My group uses X-ray crystallography as a central technique to study the structure-function relationships of complexes involving RNA of various kinds in eukaryotic cells. This includes the transcription/replication machinery of segmented negative strand RNA viruses (e.g. influenza), complexes involved in sorting of Pol II transcripts into their appropriate processing pathways and innate immune system pattern recognition receptors, notably the response to viral RNA via Rig-I like helicases.. Keywords: Protein-RNA recognition / aminoacyl tRNA synthetases / RNA metabolism / virus structure / influenza virus polymerase / innate immunity / Rig-I like helicases / X-ray crystallography. Subject area(s): Microbiology, Virology & Pathogens , RNA , Structural Biology & Biophysics. ...

Accepted name: serine tRNA ligase. Reaction: ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer. Other name(s): seryl-tRNA synthetase; SerRS; seryl-transfer ribonucleate synthetase; seryl-transfer RNA synthetase; seryl-transfer ribonucleic acid synthetase; serine translase. Systematic name: L-serine:tRNASer ligase (AMP-forming). Comments: This enzyme also recognizes tRNASec, the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNASec, the substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9023-48-7. References:. 1. Katze, J.R. and Konigsberg, W. Purification and properties of seryl transfer ribonucleic acid synthetase from Escherichia coli. J. Biol. Chem. 245 (1970) 923-930. [PMID: 4906848]. 2. Makman, M.H. and Cantoni, G.L. Isolation of seryl and phenylalanyl ribonucleic acid synthetases from bakers yeast. Biochemistry 4 (1965) 1434-1442.. 3. Webster, L.T. and ...

TY - JOUR. T1 - Autoantibodies to aminoacyl-tRNA synthetases. AU - Hirakata, Michito. PY - 2005/6. Y1 - 2005/6. KW - Aminoacyl transfer RNA synthetases. KW - Autoantibodies. KW - Interstitial lung diseases. KW - Myositis. UR - http://www.scopus.com/inward/record.url?scp=21644464398&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=21644464398&partnerID=8YFLogxK. U2 - 10.2169/internalmedicine.44.527. DO - 10.2169/internalmedicine.44.527. M3 - Editorial. C2 - 16020871. AN - SCOPUS:21644464398. VL - 44. SP - 527. EP - 528. JO - Internal Medicine. JF - Internal Medicine. SN - 0918-2918. IS - 6. ER - ...

Figure 1: A parallel genetic code. There are several major challenges in genetically encoding multiple unnatural amino acids into proteins in living cells. First, unique new codons are required that can be used to encode the incorporation of unnatural amino acids at specific sites in proteins. Since the 64 triplet codons are used in the genome of most organisms for encoding natural proteins additional codons (such as quadruplet codons) might be used to encode the incorporation of unnatural amino acids. Second, new aminoacyl-tRNA synthetase tRNA pairs that are orthogonal to the aminoacyl-tRNA synthetase/tRNA pairs in the host organism, and that uniquely direct the incorporation of an unnatural amino acid in response to a unique codon, are required. Finally the scope of cellular protein translation is limited to alpha-L amino acids and their close analogs, and alteration of the ribosome and potentially other components of the translational machinery are required to increase the chemical scope of ...

Aminoacyl tRNA synthetase (aaRS) or tRNA ligase catalyzes the esterification of a specific amino acid to its cognate tRNA to form an aminoacyl-tRNA. The amino acid is transferred by the ribosome from the aminoacylated-tRNA onto a growing polypeptide chain. Class I of aaRS is a monomer or dimer, it has 2 highly conserved sequence motifs and it aminoacylates at the 2-OH of an adenosine nucleotide. Class II of aaRS is a dimer or tetramer, it has 3 highly conserved sequence motifs and it aminoacylates at the 3-OH of an adenosine nucleotide. CP1 domain of RS edits a mischarged aa-tRNA. Some of the crystal structures are complexes of the RS with their reactant analog: amino acid-sulfamoyl adenine (aa-SA).[1]. ...

Background Aminoacyl-tRNA synthetases (AARSs) catalyze the first step of protein synthesis. We also established a strategy to check the natural activity of rhTyrRS by calculating aminoacylation and IL-8 launch in rhTyrRS-treated HL-60 cells. Conclusions The characterization of purified rhTyrRS indicated that proteins could be found in pharmacokinetic and pharmacodynamic research. and animal research could possibly be carried out to judge its toxic and pharmacologic results then. In this scholarly study, rhTyrRS was indicated at a higher level in and purified for potential preclinical testing. Strategies Cells and antibodies The skilled stress BL21 (F-ompT hsdS (rB-mB-) gal dcm; providded by aTyr Pharma) was utilized as the sponsor for rhTyrRS manifestation. This stress was transformed using the pET24a inducible manifestation vector where the His-tag series was deleted as well as the T7 promoter was changed having a Tac promoter. A mouse anti-human IL-8 monoclonal antibody ...

QARS, DARS, KARS. The current publication by Zhang and collaborators give us an interesting refresher course on basic molecular biology, particularly a section of the cellular machinery that I didnt believe to be relevant to human genetic epilepsies - tRNAs. In humans the amino acids are attached to the tRNAs through 37 different forms of tRNA synthetases, 17 of them only present in mitochondria. The names of the tRNA synthetases is derived from the specific amino acid symbol, followed by the suffix -ARS. Amongst the various tRNA synthetases implicated in human disease, two disease-related aaRS occur in a functional complex with QARS, the multisynthetase complex. These two aaRS are KARS and DARS. The KARS gene coding for the lysine tRNA synthetase has been found to be mutated in a particular form of Charcot-Marie-Tooth disease and, separately from this, nonsyndromic hearing loss. Mutations in the DARS gene coding for the asparate tRNA synthetase cause an inherited white matter disorder with leg ...

aminoacyl tRNA synthetase p18 component: shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1; amino acid sequence given in first source

Chemistry of Aminoacyl-tRNA Synthetases - CHEMICAL BIOLOGY - reflects the multidimensional character of chemical biology, focusing in particular on the fundamental science of biological structures and systems, the use of chemical and biological techniques to elucidate

TY - JOUR. T1 - Signaling pathways for TNF production induced by human aminoacyl-tRNA synthetase-associating factor, p43. AU - Park, Heonyong. AU - Park, Sang Gyu. AU - Kim, Junghee. AU - Ko, Young Gyu. AU - Kim, Sunghoon. PY - 2002/11. Y1 - 2002/11. N2 - The p43 protein is associated with human macromolecular aminoacyl tRNA synthetase complex and secreted to up-regulate diverse proinflammatory genes including TNF. Here we focused on the p43-induced TNF production and determined its responsible signal pathway. The p43-induced TNF production was mediated by the activation of MAPK family members, ERK and p38 MAPK, and by IκB degradation leading to the activation of NFκB. We also studied the upstream molecules for ERK and p38 MAPK by using a variety of inhibitors. The inhibitors for protein kinase C (PKC) and phospholipase C (PLC) prevented the p43-induced TNF production. Interestingly, all of the effective drugs inhibited the ERK activity, while the drugs had no effects on p38 MAPK activity and ...

Eprs - mouse gene knockout kit via CRISPR, 1 kit. |dl||dt|Kit Component:|/dt||dd|- |strong|KN305300G1|/strong|, Eprs gRNA vector 1 in |a href=http://www.origene.com/CRISPR-CAS9/Detail.

Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation ...

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InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.

Appropriate attachment of an amino acid to its cognate tRNA is the key to faithful translation of the genetic code. The family of enzymes responsible for this is the aminoacyl-tRNA synthetases (AATRSs) (EC 6.1.1.-). AATRSs catalyse a two-step reaction: (1) Enzyme + amino acid + ATP ---> Enzyme(aminoacyl-AMP) + PPi (2) tRNA + Enzyme(aminoacyl-AMP) ---> aminoacyl-tRNA + AMP + Enzyme In the first step, they form an aminoacyl-adenylate, in which the carboxyl of the amino acid is linked to the alpha-phosphate of ATP, by displacing the pyrophosphate. When the correct tRNA is bound, the aminoacyl group is transferred to the 2- or 3-terminal OH of the tRNA at the expense of AMP [1]. Based on structural and sequence comparisons, this group of at least 20 proteins (in prokaryotes there are approximately 20, but in eukaryotes there are usually 2 forms for each amino acid; namely, the cytosolic and mitochondrial forms) can be divided into two classes. Class I AATRSs contain a characteristic Rossman fold ...

Phylogenetic analysis of aminoacyl-tRNA synthetases (aaRSs) of all 20specificities from completely sequenced bacterial, archaeal, andeukaryotic genomes reveals a complex evolutionary picture. Detailedexamination of the domain architecture of aaRSs using sequence profilesearches delineated a network of partially conserved domains that is evenmore elaborate than previously suspected. Several unexpected evolutionaryconnections were identified, including the apparent origin of thebeta-subunit of bacterial GlyRS from the HD superfamily of hydrolases, adomain shared by bacterial AspRS and the B subunit of archaealglutamyl-tRNA amidotransferases, and another previously undetected domainthat is conserved in a subset of ThrRS, guanosine polyphosphate hydrolasesand synthetases, and a family of GTPases. Comparison of domainarchitectures and multiple alignments resulted in the delineation ofsynapomorphies-shared derived characters, such as extra domains orinserts-for most of the aaRSs specificities. These ...

Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with…

Leu-AMS (compound 6)，亮氨酸类似物，是一种有效的亮氨酰-tRNA 合成酶 (LRS) 抑制剂，IC50 值为 22.34 nM，Leu-AMS 抑制了LRS 的催化活性，但不影响亮氨酸诱导的 mTORC1 活化。Leu-AMS在癌细胞和正常细胞中显示出细胞毒性，并抑制细菌的生长 ...

Semantic Scholar extracted view of [14C]erythromycin-ribosome complex formation and non-enzymatic binding of aminoacyl-transfer RNA to ribosome-messenger RNA complex. by Kohichi Tanaka et al.

Rabbit polyclonal Glutamyl Prolyl tRNA synthetase antibody validated for WB, IHC and tested in Human. With 4 independent reviews. Immunogen corresponding to…

Mouse monoclonal valyl tRNA synthetase antibody [VARSA7E6] validated for WB, Dot and tested in Human. Immunogen corresponding to recombinant fragment

This disclosure provides variants of the biphenylalanine (BipA) orthogonal translation system used for incorporation of BipA into proteins. Specifically, engineered BipA aminoacyl-tRNA synthetase (BipARS) variants and tRNA variants that improve selectivity towards BipA are described. Furthermore, this disclosure provides methods used to generate these variants.

Plasmid pDULE-ABK from Dr. Peter Schultzs lab contains the inserts tRNA synthetase and tRNA for a photocrosslinking amino acid and is published in Chembiochem. 2011 Aug 16;12(12):1854-7. doi: 10.1002/cbic.201100194. Epub 2011 Jun 15. This plasmid is available through Addgene.

Looking for online definition of aminoacyl-tRNA synthetases in the Medical Dictionary? aminoacyl-tRNA synthetases explanation free. What is aminoacyl-tRNA synthetases? Meaning of aminoacyl-tRNA synthetases medical term. What does aminoacyl-tRNA synthetases mean?

Histidyl-tRNA synthetase (HARS) also known as histidine-tRNA ligase, is an enzyme which in humans is encoded by the HARS gene. Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis. HARS has been shown to interact with EEF1B2 and EEF1G. GRCh38: Ensembl release 89: ENSG00000170445 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000001380 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Entrez Gene: HARS ...

TY - JOUR. T1 - Methionine Analogue Probes Functionally Important Residues in Active Site of Methionyl-tRNA Synthetase. AU - Jo, Yeong Joon. AU - Lee, Sang Won. AU - Jo, Myung Kyun. AU - Lee, Jee Woo. AU - Kang, Mee Kyoung. AU - Yoon, Jeong Hyeok. AU - Kim, Sunghoon. PY - 1999/11/30. Y1 - 1999/11/30. N2 - Aminoacyl-tRNA synthetases are essential enzymes catalyzing the attachment of specific amino acids to cognate tRNAs. In the present work, the substrate analogue L-methionine hydroxamate was used to identify functional residues located in the active site of the E. coli methionyl-tRNA synthetase (MetRS). This compound inhibited bacteria, yeast, and human MetRS activities to a similar degree, suggesting a conserved active site structure and mechanism between MetRSs of different phylogenetic domains. Mutants of the E. coli MetRS resistant to methionine hydroxamate were also isolated. These mutants contained a substitution either at T10, Y15, or Y94. These residues are highly conserved among the ...

Using fluorescent antibody staining, we have established the association of methionyl-tRNA synthetase with the endoplasmic reticulum in PtK2 cells. After Triton X-100 extraction, 70% of the recovered aminoacyl-tRNA synthetase activity was found in the detergent-insoluble fraction. This fraction of the enzyme remained localized with insoluble endoplasmic reticulum antigens and with ribosomes, which were stained with acridine orange. By both fluorescence microscopy and electron microscopy the organization of the detergent-insoluble residue was found to depend on the composition of the extracting solution. After extraction with a microtubule-stabilizing buffer containing EGTA, Triton X-100, and polyethylene glycol (Osburn, M., and K. Weber, 1977, Cell, 12:561-571) the ribosomes were aggregated in large clusters with remnants of membranes. After extraction with a buffer containing Triton X-100, sucrose, and CaCl2 (Fulton, A. B., K. M. Wang, and S. Penman, 1980, Cell, 20:849-857), the ribosomes were ...

Using fluorescent antibody staining, we have established the association of methionyl-tRNA synthetase with the endoplasmic reticulum in PtK2 cells. After Triton X-100 extraction, 70% of the recovered aminoacyl-tRNA synthetase activity was found in the detergent-insoluble fraction. This fraction of the enzyme remained localized with insoluble endoplasmic reticulum antigens and with ribosomes, which were stained with acridine orange. By both fluorescence microscopy and electron microscopy the organization of the detergent-insoluble residue was found to depend on the composition of the extracting solution. After extraction with a microtubule-stabilizing buffer containing EGTA, Triton X-100, and polyethylene glycol (Osburn, M., and K. Weber, 1977, Cell, 12:561-571) the ribosomes were aggregated in large clusters with remnants of membranes. After extraction with a buffer containing Triton X-100, sucrose, and CaCl2 (Fulton, A. B., K. M. Wang, and S. Penman, 1980, Cell, 20:849-857), the ribosomes were ...

The SRP9/14 heterodimer is the latest member of a growing family of small α/β RNA binding proteins examples of which are: the ribonucleoprotein (RNP) domain (Nagai et al., 1990; Oubridge et al., 1994); the double‐stranded RNA binding domain (dsRBD) (Farrandon et al., 1994; Bycroft et al., 1995; Kharrat et al., 1995); the K homology (KH) domain (Musco et al., 1996); the coat protein of bacteriophage MS2 (Valegård et al., 1990); the translational initiation factor IF3 (Biou et al., 1995); the S1 RNA binding domain (Bycroft et al., 1997); and many ribosomal proteins (Nagai, 1996). The RNP and KH domains, as well as several ribosomal proteins (Liljas and Garber, 1995), belong to the so‐called split α‐β‐α motif differing from the dsRBD, MS2 and SRP9/14 where the sheet is a β‐meander. In aminoacyl‐tRNA synthetases, a number of different tRNA anti‐codon binding modules have also been characterized (Cusack, 1995; Moras and Poterszman, 1996). Interestingly, RNA and DNA binding ...

The in vivo, genetically programmed incorporation of designer amino acids allows the properties of proteins to be tailored with molecular precision. The Methanococcus jannaschii tyrosyl-transfer-RNA synthetase-tRNA_(CUA) (MjTyrRS-tRNA_(CUA)) and the Methanosarcina barkeri pyrrolysyl-tRNA synthetase-tRNA_(CUA) (MbPylRS-tRNA_(CUA)) orthogonal pairs have been evolved to incorporate a range of unnatural amino acids in response to the amber codon in Escherichia coli. However, the potential of synthetic genetic code expansion is generally limited to the low efficiency incorporation of a single type of unnatural amino acid at a time, because every triplet codon in the universal genetic code is used in encoding the synthesis of the proteome. To encode efficiently many distinct unnatural amino acids into proteins we require blank codons and mutually orthogonal aminoacyl-tRNA synthetase-tRNA pairs that recognize unnatural amino acids and decode the new codons. Here we synthetically evolve an orthogonal ...

TY - JOUR. T1 - Isolated CP1 domain of Escherichia coli leucyl-tRNA synthetase is dependent on flanking hinge motifs for amino acid editing activity. AU - Betha, Aswini K.. AU - Williams, Amy M.. AU - Martinis, Susan A.. PY - 2007/5/29. Y1 - 2007/5/29. N2 - Protein synthesis and its fidelity rely upon the aminoacyl-tRNA synthetases. Leucyl-tRNA synthetase (LeuRS), isoleucyl-tRNA synthetase (IleRS), and valyl-tRNA synthetase (ValRS) have evolved a discrete editing domain called CP1 that hydrolyzes the respective incorrectly misaminoacylated noncognate amino acids. Although active CP1 domain fragments have been isolated for IleRS and ValRS, previous reports suggested that the LeuRS CP1 domain required idiosyncratic adaptations to confer editing activity independent of the full-length enzyme. Herein, characterization of a series of rationally designed Escherichia coli LeuRS fragments showed that the β-strands, which link the CP1 domain to the aminoacylation core of LeuRS, are required for editing ...

In enzymology , a valine-tRNA ligase ( EC 6.1.1.9 ) is an enzyme that catalyzes the chemical reaction The 3 substrates of this enzyme are ATP , L-valine , and tRNA(Val) , whereas its 3 products are AMP , diphosphate , and L-valyl-tRNA(Val) . This enzyme belongs to the family of ligases , to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-valine:tRNAVal ligase (AMP-forming) . Other names in common use include valyl-tRNA synthetase , valyl-transfer ribonucleate synthetase , valyl-transfer RNA synthetase , valyl-transfer ribonucleic acid synthetase , valine transfer ribonucleate ligase , and valine translase . This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis . Structural studies As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GAX , 1IVS , 1IYW , 1WK9 , and 1WKA . See also VARS References Berg P, Bergmann FH, Ofengand

Because of previous data suggesting that aminoacyl-tRNA synthetases make a transient Michael adduct with a specific uridine residue in the tRNA structure, (Schoemaker, H.J.P., and Schimmel, P.R. (1977) Biochemistry 16, 5454-5460) attempts were made to find simple model systems in which this reaction might be studied in more detail. In the course of these investigations, it was found that Escherichia coli Ile-tRNA synthetase catalyzes cleavage of the glycosidic bond of 5-bromouridine. At pH 7.5, ambient temperatures, the turnover number is roughly 5/h. 5-Fluoro-, 5-chloro-, and 5-iodouridine are also cleaved in an analogous way by Ile-tRNA synthetase. In the case of uridine, conversion of uridine to uracil and ribose was also detected, but with a smaller turnover number. Three other E. coli and one mammalian aminoacyl-tRNA synthetases were also examined and all were found to catalyze glycosidic bond cleavage of 5-bromouridine. The data indicate that, in general, synthetases have a catalytic ...

Build: Wed Jun 21 18:33:50 EDT 2017 (commit: 4a3b2dc). National Center for Advancing Translational Sciences (NCATS), 6701 Democracy Boulevard, Bethesda MD 20892-4874 • 301-435-0888. ...

The genetic code is brought into action by 20 aminoacyl-tRNA synthetases. These enzymes are evenly divided into two classes (I and II) that recognize tRNAs from the minor and major groove sides of the acceptor stem, respectively. We have reported recently that: (1) ribozymic precursors of the synthetases seem to have used the same two sterically mirror modes of tRNA recognition, (2) having these two modes might have helped in preventing erroneous aminoacylation of ancestral tRNAs with complementary anticodons, yet (3) the risk of confusion for the presumably earliest pairs of complementarily encoded amino acids had little to do with anticodons. Accordingly, in this communication we focus on the acceptor stem. Our main result is the emergence of a palindrome structure for the acceptor stems common ancestor, reconstructed from the phylogenetic trees of Bacteria, Archaea and Eukarya. In parallel, for pairs of ancestral tRNAs with complementary anticodons, we present updated evidence of concerted

Amino acid starvation activates the protein kinase Gcn2p, leading to changes in gene expression and translation. Gcn2p is activated by deacylated tRNA, which accumulates when tRNA aminoacylation is limited by lack of substrates or inhibition of synthesis. Pairing of amino acids and deacylated tRNAs is catalyzed by aminoacyl-tRNA synthetases, which use quality control pathways to maintain substrate specificity. Phenylalanyl-tRNA synthetase (PheRS) maintains specificity via an editing pathway that targets non-cognate Tyr-tRNAPhe. While the primary role of aaRS editing is to prevent misaminoacylation, we demonstrate editing of misaminoacylated tRNA is also required for detection of amino acid starvation by Gcn2p. Ablation of PheRS editing caused accumulation of Tyr-tRNAPhe (5%), but not deacylated tRNAPhe during amino acid starvation, limiting Gcn2p kinase activity and suppressing Gcn4p-dependent gene expression. While the PheRS-editing ablated strain grew 50% slower and displayed a 27-fold increase in the

This invention provides methods and compositions for incorporation of an unnatural amino acid into a peptide using an orthogonal aminoacyl tRNA synthetase/tRNA pair. In particular, an orthogonal pair

In plants, the stem cells that form the shoot system reside within the shoot apical meristem (SAM), which is regulated by feedback signaling between the WUSCHEL (WUS) homeobox protein and CLAVATA (CLV) peptides and receptors. WUS-CLV feedback signaling can be modulated by various endogenous or exogenous factors such as chromatin state, hormone signaling, reactive oxygen species (ROS) signaling and nutrition, leading to a dynamic control of SAM size corresponding to meristem activity. Despite these insights, however, the knowledge of genes that control SAM size is still limited, and in particular the regulation by ROS signaling is only beginning to be comprehended. Here, we report a new gene that functions in SAM size maintenance, OKINA KUKI (OKI1), which is expressed in the SAM and encodes a mitochondrial aspartyl tRNA synthetase (AspRS). oki1 mutants display enlarged SAMs with abnormal expression of WUS and CLV3, and overaccumulation of ROS in the meristem. Our findings support the importance ...

The rapid progress of research in the tRNA field and recent advances in the understanding of the molecular basis of specificity in tRNA: protein interactions make it necessary to have all of the accumulated information in an easily accessible form. The purpose of this book is to fulfill that need by providing an up-to-date account of all aspects of research on transfer RNA, including its structure, biosynthesis, and interactions with the many proteins involved in protein biosynthesis. Beginning with an historical account, the book covers a broad area of research on tRNA biosynthesis, the different functions of tRNA in the genetic decoding process, its association with many different proteins, and the emerging rules governing the specificity of their interactions. In view of the impressive progress made in the last few years, several of the chapters are devoted to discussion of aminoacyl-tRNA synthetase tRNA interactions. An appendix containing the structural formulae of all modified nucleosides found in

Aminoacyl-tRNA synthetases (aaRSs) are modular enzymes globally conserved in the three kingdoms of life. All catalyze the same two-step reaction, i.e., the attachment of a proteinogenic amino acid on their cognate tRNAs, thereby mediating the correct expression of the genetic code. In addition, some aaRSs acquired other functions beyond this key role in translation. Genomics and X-ray crystallography have revealed great structural diversity in aaRSs (e.g., in oligomery and modularity, in ranking into two distinct groups each subdivided in 3 subgroups, by additional domains appended on the catalytic modules). AaRSs show huge structural plasticity related to function and limited idiosyncrasies that are kingdom or even species specific (e.g., the presence in many Bacteria of non discriminating aaRSs compensating for the absence of one or two specific aaRSs, notably AsnRS and/or GlnRS). Diversity, as well, occurs in the mechanisms of aaRS gene regulation that are not conserved in evolution, notably ...

Complete information for CARS2 gene (Protein Coding), Cysteinyl-TRNA Synthetase 2, Mitochondrial, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

JUPITER, FL - For the past several years, Min Guo, an assistant professor at The Scripps Research Institute (TSRI), has focused on the intricate actions of an ancient family of catalytic enzymes that play a key role in translation, the process of producing proteins. These complex enzymes are a group of fundamental molecules that make building blocks for protein production. Present in every cell, these enzymes-known as aminoacyl-transfer RNA synthetases (tRNA synthetases)-select the proper amino acids and assign them to transfer RNAs to make a protein in the ribosome. As an essential step of determining the genetic code, tRNA synthetases have been around for billions of years. However, this essential part of the protein-making machine did not stop evolving. Now, in a new study published online ahead of print on November 15, 2012, by the journal Molecular Cell, Guo, Ehud Razin of The Institute for Medical Research Israel-Canada, and a large team of international scientists have shown that this ...

PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.

Complete information for PARS2 gene (Protein Coding), Prolyl-TRNA Synthetase 2, Mitochondrial, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

Glutamyl-prolyl-tRNA synthetase. (Aliases: AATS,GluProRS,Aa-tRNA-syn-glupro,ERS,AATs-GluPro,CG5394,GluRS,glutamyl-prolyl-tRNA synthetase,Aats-glu,p200,aminoacyl-tRNA synthetase,GluPro-RS,EPRS,Dmel\CG5394) ...

Mouse Monoclonal Anti-Tryptophanyl tRNA synthetase Antibody (3A12) [PE]. Validated: WB, ELISA, ICC/IF, IP. Tested Reactivity: Human. 100% Guaranteed.

Mouse Monoclonal Anti-Seryl tRNA synthetase Antibody (1H4) [DyLight 488]. Validated: WB, ELISA, ICC/IF, IHC, IHC-P. Tested Reactivity: Human. 100% Guaranteed.

Adenosine monophosphate (AMP) is a key cellular metabolite regulating energy homeostasis and signal transduction. AMP is also a product of various enzymatic reactions, many of which are dysregulated during disease conditions. Thus, monitoring the activities of these enzymes is a primary goal for developing modulators for these enzymes. In this study, we demonstrate the versatility of an enzyme-coupled assay that quantifies the amount of AMP produced by any enzymatic reaction regardless of its substrates. We successfully implemented it to enzyme reactions that use adenosine triphosphate (ATP) as a substrate (aminoacyl tRNA synthetase and DNA ligase) by an elaborate strategy of removing residual ATP and converting AMP produced into ATP; so it can be detected using luciferase/luciferin and generating light ...

Article{pmid25409537, Author=Thibodeaux, C. J. and Ha, T. and van der Donk, W. A. , Title={{A} price to pay for relaxed substrate specificity: a comparative kinetic analysis of the class {I}{I} lanthipeptide synthetases {P}roc{M} and {H}al{M}2}, Journal=J. Am. Chem. Soc., Year=2014, Volume=136, Number=50, Pages=17513--17529, Month=Dec ...

Antibodies for proteins involved in ligase activity, forming aminoacyl-tRNA and related compounds pathways, according to their Panther/Gene Ontology Classification

Aliases : GRMZM2G078756. Description : 29.1.20 protein.aa activation.phenylalanine-tRNA ligase phenylalanyl-tRNA synthetase class IIc family protein. ...

K.NAKANISHI,Y.OGISO,T.NAKAMA,S.FUKAI,O.NUREKI. CRYSTAL STRUCTURE OF AQUIFEX AEOLICUS METHIONYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(MET) AND METHIONYL-ADENYLATE ANOLOGUE. TO BE PUBLISHED ...

July 15 2017 Issue The semi-monthly AARS online Hot Topics Newsletter is an exclusive AARS member benefit! You dont need to spend countless hours perusing your typical online sources when you have this! Stay informed today by becoming an AARS member and receiving the Hot Topics!

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