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tRNA Synthetase

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https://www.readbyqxmd.com/read/29332387/proteome-wide-characterization-of-phosphorylation-induced-conformational-changes-in-breast-cancer
#1
He Meng, Michael C Fitzgerald
Because of the close link between protein function and protein folding stability, knowledge about phosphorylation-induced protein folding stability changes can lead to a better understanding of the functional effects of protein phosphorylation. Here, the Stability of Proteins from Rates of OXidation (SPROX) and Limited Proteolysis (LiP) techniques are used to compare the conformational properties of proteins in two MCF-7 cell lysates, including one that was and one that was not dephosphorylated with alkaline phosphatase...
January 15, 2018: Journal of Proteome Research
https://www.readbyqxmd.com/read/29328069/inhibition-of-muc1-biosynthesis-via-threonyl-trna-synthetase-suppresses-pancreatic-cancer-cell-migration
#2
Seung Jae Jeong, Jong Hyun Kim, Beom Jin Lim, Ina Yoon, Ji-Ae Song, Hee-Sun Moon, Doyeun Kim, Dong Ki Lee, Sunghoon Kim
Mucin1 (MUC1), a heterodimeric oncoprotein, containing tandem repeat structures with a high proportion of threonine, is aberrantly overexpressed in many human cancers including pancreatic cancer. Since the overall survival rate of pancreatic cancer patients has remained low for several decades, novel therapeutic approaches are highly needed. Intestinal mucin has been known to be affected by dietary threonine supply since de novo synthesis of mucin proteins is sensitive to luminal threonine concentration. However, it is unknown whether biosynthesis of MUC1 is regulated by threonine in human cancers...
January 12, 2018: Experimental & Molecular Medicine
https://www.readbyqxmd.com/read/29320932/classical-molecular-dynamics-simulation-of-seryl-trna-synthetase-and-threonyl-trna-synthetase-bound-with-trna-and-aminoacyl-adenylate
#3
Saheb Dutta, Nilashis Nandi
Lacunae of understanding exist concerning the active site organization during the charging step of the aminoacylation reaction. We present here a molecular dynamics simulation study of the dynamics of the active site organization during charging step of subclass IIa dimeric SerRS from Thermus thermophilus (ttSerRS) bound with tttRNASer and dimeric ThrRS from Escherichia coli (ecThrRS) bound with ectRNAThr. The interactions between the catalytically important loops and tRNA contribute to the change in dynamics of tRNA in free and bound states, respectively...
January 10, 2018: Journal of Biomolecular Structure & Dynamics
https://www.readbyqxmd.com/read/29320701/aminoacylation-of-proteins-new-targets-for-the-old-arsenal
#4
Seyed Mehdi Jafarnejad, Sung-Hoon Kim, Nahum Sonenberg
Besides charging tRNAs with their cognate amino acids, aminoacyl-tRNA synthetases (ARSs) are involved in a plethora of non-canonical functions, including development, immune response, and angiogenesis. In this issue of Cell Metabolism, He et al. (2018) report a novel biochemical function of ARSs: posttranslational addition of amino acids to lysine residues in proteins.
January 9, 2018: Cell Metabolism
https://www.readbyqxmd.com/read/29314548/clinical-biochemical-and-genetic-features-associated-with-vars2-related-mitochondrial-disease
#5
Francesco Bruni, Ivano Di Meo, Emanuele Bellacchio, Bryn D Webb, Robert McFarland, Zofia M A Chrzanowska-Lightowlers, Langping He, Ewa Skorupa, Isabella Moroni, Anna Ardissone, Anna Walczak, Henna Tyynismaa, Pirjo Isohanni, Hanna Mandel, Holger Prokisch, Tobias Haack, Penelope E Bonnen, Bertini Enrico, Ewa Pronicka, Daniele Ghezzi, Robert W Taylor, Daria Diodato
In recent years, an increasing number of mitochondrial disorders have been associated with mutations in mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs), which are key enzymes of mitochondrial protein synthesis. Bi-allelic functional variants in VARS2, encoding the mitochondrial valyl tRNA-synthetase, were first reported in a patient with psychomotor delay and epilepsia partialis continua associated with an oxidative phosphorylation (OXPHOS) complex I defect, before being described in a patient with a neonatal form of encephalocardiomyopathy...
January 3, 2018: Human Mutation
https://www.readbyqxmd.com/read/29305884/aminoacyl-trna-synthetases-structure-function-and-drug-discovery
#6
REVIEW
Vijayakumar Rajendran, Parismita Kalita, Harish Shukla, Awanish Kumar, Timir Tripathi
Aminoacyl-tRNA synthetases (AARSs) are the enzymes that catalyze the aminoacylation reaction by covalently linking an amino acid to its cognate tRNA in the first step of protein translation. Beyond this classical function, these enzymes are also known to have a role in several metabolic and signaling pathways that are important for cell viability. Study of these enzymes is of great interest to the researchers due to its pivotal role in the growth and survival of an organism. Further, unfolding the interesting structural and functional aspects of these enzymes in the last few years has qualified them as a potential drug target against various diseases...
January 3, 2018: International Journal of Biological Macromolecules
https://www.readbyqxmd.com/read/29301968/engineering-posttranslational-proofreading-to-discriminate-nonstandard-amino-acids
#7
Aditya M Kunjapur, Devon A Stork, Erkin Kuru, Oscar Vargas-Rodriguez, Matthieu Landon, Dieter Söll, George M Church
Incorporation of nonstandard amino acids (nsAAs) leads to chemical diversification of proteins, which is an important tool for the investigation and engineering of biological processes. However, the aminoacyl-tRNA synthetases crucial for this process are polyspecific in regard to nsAAs and standard amino acids. Here, we develop a quality control system called "posttranslational proofreading" to more accurately and rapidly evaluate nsAA incorporation. We achieve this proofreading by hijacking a natural pathway of protein degradation known as the N-end rule, which regulates the lifespan of a protein based on its amino-terminal residue...
January 4, 2018: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/29289698/tyrosyl-trna-synthetase-a-potential-kyotorphin-synthetase-in-mammals
#8
Tamotsu Tsukahara, Shuhei Yamagishi, Hiroyuki Neyama, Hiroshi Ueda
Kyotorphin (KTP; L-tyrosyl-L-arginine), an opioid-like analgesic discovered in the bovine brain, is potentially a neuromodulator because of its localization in synaptosomes, the existence of a specific KTP receptor, and the presence of its biosynthetic enzyme in the brain. KTP is formed in the brain from its constituent amino acids, L-tyrosine and L-arginine, by an enzyme termed KTP synthetase. However, the latter has never been identified. We aimed to test the hypothesis that tyrosyl-tRNA synthetase (TyrRS) is also KTP synthetase...
December 28, 2017: Peptides
https://www.readbyqxmd.com/read/29289262/clinical-heterogeneity-of-interstitial-lung-disease-in-polymyositis-and-dermatomyositis-patients-with-or-without-specific-autoantibodies
#9
Fang Chen, Shanshan Li, Tao Wang, Jingli Shi, Guochun Wang
BACKGROUND: The aim of this study was to compare the heterogeneity of interstitial lung disease (ILD) in patients with polymyositis and dermatomyositis (PM/DM) according to serological type. METHODS: A total of 182 patients with PM/DM-ILD were observed retrospectively. Antiaminoacyl-tRNA synthetase (ARS) and antimelanoma differentiation-associated gene5 (MDA5) antibodies were screened using immunoblotting approach. The patients with ILD were divided into 3 groups: MDA5 (with anti-MDA5 antibody), ARS (with anti-ARS antibody) and MSN (without anti-MDA5 or anti-ARS antibody) group...
January 2018: American Journal of the Medical Sciences
https://www.readbyqxmd.com/read/29288497/the-role-of-trna-synthetases-in-neurological-and-neuromuscular-disorders
#10
REVIEW
Veronika Boczonadi, Matthew J Jennings, Rita Horvath
Aminoacyl-tRNA synthetases (ARSs) are ubiquitously expressed enzymes responsible for charging tRNAs with their cognate amino acids, therefore essential for the first step in protein synthesis. Although the majority of protein synthesis happens in the cytosol, an additional translation apparatus is required to translate the 13 mitochondrial DNA-encoded proteins important in oxidative phosphorylation. Most ARS genes in these cellular compartments are distinct, but two genes are common, encoding aminoacyl-tRNA synthetases of glycine (GARS) and lysine (KARS) in both mitochondria and the cytosol...
December 30, 2017: FEBS Letters
https://www.readbyqxmd.com/read/29286490/a-facile-protocol-to-generate-site-specifically-acetylated-proteins-in-escherichia-coli
#11
Sumana Venkat, Caroline Gregory, Kexin Meng, Qinglei Gan, Chenguang Fan
Post-translational modifications that occur at specific positions of proteins have been shown to play important roles in a variety of cellular processes. Among them, reversible lysine acetylation is one of the most widely distributed in all domains of life. Although numerous mass spectrometry-based acetylome studies have been performed, further characterization of these putative acetylation targets has been limited. One possible reason is that it is difficult to generate purely acetylated proteins at desired positions by most classic biochemical approaches...
December 9, 2017: Journal of Visualized Experiments: JoVE
https://www.readbyqxmd.com/read/29281289/unraveling-the-critical-role-played-by-ado762-oh-in-the-post-transfer-editing-by-archaeal-threonyl-trna-synthetase
#12
Mohamed M Aboelnga, John J Hayward, James W Gauld
Archaeal threonyl-tRNA synthetase (ThrRS) possesses an editing active site wherein tRNAThr that has been misaminoacylated with serine (i.e., Ser-tRNAThr) is hydrolytically cleaved to serine and tRNAThr. It has been suggested that the free ribose sugar hydroxyl of Ado76 of the tRNAThr (Ado762'OH) is the mechanistic base, promoting hydrolysis by orienting a nucleophilic water near the scissile Ser-tRNAThr ester bond. We have performed a computational study, involving Molecular Dynamics (MD) and hybrid ONIOM Quantum Mechanics/Molecular Mechanics (QM/MM) methods, considering all possible editing mechanisms in order to gain an understanding of the role played by Ado762'OH group...
December 27, 2017: Journal of Physical Chemistry. B
https://www.readbyqxmd.com/read/29273753/double-mimicry-evades-trna-synthetase-editing-by-toxic-vegetable-sourced-non-proteinogenic-amino-acid
#13
Youngzee Song, Huihao Zhou, My-Nuong Vo, Yi Shi, Mir Hussain Nawaz, Oscar Vargas-Rodriguez, Jolene K Diedrich, John R Yates, Shuji Kishi, Karin Musier-Forsyth, Paul Schimmel
Hundreds of non-proteinogenic (np) amino acids (AA) are found in plants and can in principle enter human protein synthesis through foods. While aminoacyl-tRNA synthetase (AARS) editing potentially provides a mechanism to reject np AAs, some have pathological associations. Co-crystal structures show that vegetable-sourced azetidine-2-carboxylic acid (Aze), a dual mimic of proline and alanine, is activated by both human prolyl- and alanyl-tRNA synthetases. However, it inserts into proteins as proline, with toxic consequences in vivo...
December 22, 2017: Nature Communications
https://www.readbyqxmd.com/read/29273296/an-archaeal-aminoacyl-trna-synthetase-complex-for-improved-substrate-quality-control
#14
Ana Crnković, Mirela Čavužić, Vlatka Godinić-Mikulčić, Gregor Anderluh, Ivana Weygand-Đurašević, Ita Gruić-Sovulj
Aminoacyl-tRNA synthetases (aaRS) decode genetic information by coupling tRNAs with cognate amino acids. In the archaeon Methanothermobacter thermautotrophicus arginyl- and seryl-tRNA synthetase (ArgRS and SerRS, respectively) form a complex which enhances serylation and facilitates tRNASer recycling through its association with the ribosome. Yet, the way by which complex formation participates in Arg-tRNAArg synthesis is still unresolved. Here we utilized pull down and surface plasmon resonance experiments with truncated ArgRS variants to demonstrate that ArgRS uses its N-terminal domain to establish analogous interactions with both SerRS and cognate tRNAArg, providing a rationale for the lack of detectable SerRS•[ArgRS•tRNAArg] complex...
December 19, 2017: Biochimie
https://www.readbyqxmd.com/read/29261326/mutant-wars2-gene-in-spontaneously-hypertensive-rats-impairs-brown-adipose-tissue-function-and-predisposes-to-visceral-obesity
#15
M Pravenec, V Zídek, V Landa, P Mlejnek, J Šilhavý, M Šimáková, J Trnovská, V Škop, I Marková, H Malínská, M Hüttl, L Kazdová, K Bardová, K Tauchmannová, M Vrbacký, H Nůsková, T Mráček, J Kopecký, J Houštěk
Brown adipose tissue (BAT) plays an important role in lipid and glucose metabolism in rodents and possibly also in humans. Identification of genes responsible for BAT function would shed light on underlying pathophysiological mechanisms of metabolic disturbances. Recent linkage analysis in the BXH/HXB recombinant inbred (RI) strains, derived from Brown Norway (BN) and spontaneously hypertensive rats (SHR), identified two closely linked quantitative trait loci (QTL) associated with glucose oxidation and glucose incorporation into BAT lipids in the vicinity of Wars2 (tryptophanyl tRNA synthetase 2 (mitochondrial)) gene on chromosome 2...
December 20, 2017: Physiological Research
https://www.readbyqxmd.com/read/29259316/correction-of-a-disease-mutation-using-crispr-cas9-assisted-genome-editing-in-japanese-black-cattle
#16
Mitsumi Ikeda, Shuichi Matsuyama, Satoshi Akagi, Katsuhiro Ohkoshi, Sho Nakamura, Shiori Minabe, Koji Kimura, Misa Hosoe
Isoleucyl-tRNA synthetase (IARS) syndrome is a recessive disease of Japanese Black cattle caused by a single nucleotide substitution. To repair the mutated IARS gene, we designed clustered regularly interspaced short palindromic repeats (CRISPR)/CRISPR-associated protein 9 (Cas9) to create a double-strand break near the mutation site. CRISPR/Cas9 and donor DNA that contained a synonymous codon for the correct amino acid and an Aequorea coerulescens Green Fluorescent Protein (AcGFP) cassette with a piggyBac transposase recognition site at both ends were introduced into bovine fetal fibroblast (BFF) cells isolated from a homozygous mutant calf...
December 19, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29251727/labeling-and-identifying-cell-specific-proteomes-in-the-mouse-brain
#17
Toke P Krogager, Russell J Ernst, Thomas S Elliott, Laura Calo, Václav Beránek, Ernesto Ciabatti, Maria Grazia Spillantini, Marco Tripodi, Michael H Hastings, Jason W Chin
We develop an approach to tag proteomes synthesized by specific cell types in dissociated cortex, brain slices, and the brains of live mice. By viral-mediated expression of an orthogonal pyrrolysyl-tRNA synthetase-tRNAXXX pair in a cell type of interest and providing a non-canonical amino acid with a chemical handle, we selectively label neuronal or glial proteomes. The method enables the identification of proteins from spatially and genetically defined regions of the brain.
December 18, 2017: Nature Biotechnology
https://www.readbyqxmd.com/read/29235198/substrate-interaction-defects-in-histidyl-trna-synthetase-linked-to-dominant-axonal-peripheral-neuropathy
#18
Jamie A Abbott, Rebecca Meyer-Schuman, Vincenzo Lupo, Shawna Feely, Inès Mademan, Stephanie N Oprescu, Laurie B Griffin, M Antonia Alberti, Carlos Casasnovas, Sharon Aharoni, Lina Basel-Vanagaite, Stephan Züchner, Peter De Jonghe, Jonathan Baets, Michael E Shy, Carmen Espinós, Borries Demeler, Anthony Antonellis, Christopher Francklyn
Histidyl-tRNA synthetase (HARS) ligates histidine to cognate tRNA molecules, which is required for protein translation. Mutations in HARS cause the dominant axonal peripheral neuropathy Charcot Marie-Tooth disease type 2W (CMT2W); however, the precise molecular mechanism remains undefined. Here, we investigated three HARS missense mutations associated with CMT2W (p.Tyr330Cys, p.Ser356Asn, and p.Val155Gly). The three mutations localize to the HARS catalytic domain and failed to complement deletion of the yeast ortholog (HTS1)...
December 12, 2017: Human Mutation
https://www.readbyqxmd.com/read/29232904/an-expanded-multi-organ-disease-phenotype-associated-with-mutations-in-yars
#19
Anna Tracewska-Siemiątkowska, Lonneke Haer-Wigman, Danielle G M Bosch, Deborah Nickerson, Michael J Bamshad, Maartje van de Vorst, Nanna Dahl Rendtorff, Claes Möller, Ulrika Kjellström, Sten Andréasson, Frans P M Cremers, Lisbeth Tranebjærg
Whole exome sequence analysis was performed in a Swedish mother-father-affected proband trio with a phenotype characterized by progressive retinal degeneration with congenital nystagmus, profound congenital hearing impairment, primary amenorrhea, agenesis of the corpus callosum, and liver disease. A homozygous variant c.806T > C, p.(F269S) in the tyrosyl-tRNA synthetase gene (YARS) was the only identified candidate variant consistent with autosomal recessive inheritance. Mutations in YARS have previously been associated with both autosomal dominant Charcot-Marie-Tooth syndrome and a recently reported autosomal recessive multiorgan disease...
December 11, 2017: Genes
https://www.readbyqxmd.com/read/29229096/clinical-characteristics-of-patients-with-anti-aminoacyl-trna-synthetase-antibody-positive-idiopathic-interstitial-pneumonia
#20
Hirokazu Yura, Noriho Sakamoto, Minoru Satoh, Hiroshi Ishimoto, Tetsuya Hanaka, Chiyo Ito, Tomoko Hasegawa, Shin Tanaka, Takuto Miyamura, Shota Nakashima, Atsuko Hara, Tomoyuki Kakugawa, Keishi Oda, Takashi Kido, Yasushi Obase, Yuji Ishimatsu, Kazuhiro Yatera, Atsushi Kawakami, Hiroshi Mukae
BACKGROUND: Anti-aminoacyl-tRNA synthetase (ARS) antibodies have been detected in patients with polymyositis/dermatomyositis (PM/DM) and are especially correlated with interstitial lung disease (ILD). The aim of this study was to clarify the clinical features of patients with anti-ARS antibody positive idiopathic interstitial pneumonias (IIPs). METHODS: Patients were classified into three groups: 1) IIP with anti-ARS antibodies (ARS(+)IIP), 2) IIP without anti-ARS antibodies (ARS(-)IIP), and 3) PM/DM-associated ILD with anti-ARS antibodies (ARS(+)PM/DM-ILD)...
November 2017: Respiratory Medicine
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