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Ts translation elongation factor, mitochondrial

EF-Ts, EF-Tsmt
This gene encodes a mitochondrial translation elongation factor. The encoded protein is an enzyme that catalyzes the exchange of guanine nucleotides on the translation elongation factor Tu during the elongation step of mitchondrial protein translation. Mutations in this gene are associated with combined oxidative phosphorylation deficiency-3 syndrome. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Mar 2010] (from NCBI)
Top mentioned proteins: Elongation Factor Tu, CAN, ACID, POLYMERASE, HAD
Papers on EF-Ts
Structural basis for RNA-genome recognition during bacteriophage Qβ replication.
Knudsen et al., Århus, Denmark. In Nucleic Acids Res, Jan 2016
Upon infection of Escherichia coli by bacteriophage Qβ, the virus-encoded β-subunit recruits host translation elongation factors EF-Tu and EF-Ts and ribosomal protein S1 to form the Qβ replicase holoenzyme complex, which is responsible for amplifying the Qβ (+)-RNA genome.
Non-catalytic N-terminal domain negatively influences the nucleotide exchange activity of translation elongation factor 1Bα.
El'skaya et al., Ukraine. In Febs J, Dec 2015
UNASSIGNED: The eukaryotic translation elongation factor 1Bα (eEF1Bα) is a functional homologue of the bacterial factor EF-Ts and is a component of the macromolecular eEF1B complex.
Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu.
Knudsen et al., Århus, Denmark. In J Struct Biol, Jul 2015
Translation elongation factor EF-Tu belongs to the superfamily of guanine-nucleotide binding proteins, which play key cellular roles as regulatory switches.
Depletion of reduction potential and key energy generation metabolic enzymes underlies tellurite toxicity in Deinococcus radiodurans.
Apte et al., Mumbai, India. In Proteomics, 2015
At proteome level, tellurite resistance proteins (TerB and TerD), tellurite reducing enzymes (pyruvate dehydrogense subunits E1 and E3), ROS detoxification enzymes (superoxide dismutase and thioredoxin reductase), and protein folding chaperones (DnaK, EF-Ts, and PPIase) displayed increased abundance in tellurite-stressed cells.
Comparative secretomics reveals novel virulence-associated factors of Vibrio parahaemolyticus.
Chen et al., Shanghai, China. In Front Microbiol, 2014
In addition, comparative secretomics also revealed several extracellular proteins that have not been described in any bacteria, such as the ribosome-recycling factor, translation elongation factor EF-Ts, phosphocarrier protein HPr and maltose-binding protein MalE.
Characterization of hydrogen peroxide-resistant Acinetobacter species isolated during the Mars Phoenix spacecraft assembly.
Mogul et al., Pomona, United States. In Astrobiology, 2014
Proteomic characterizations reveal a survival mechanism inclusive of proteins coupled to peroxide degradation (catalase and alkyl hydroperoxide reductase), energy/redox management (dihydrolipoamide dehydrogenase), protein synthesis/folding (EF-G, EF-Ts, peptidyl-tRNA hydrolase, DnaK), membrane functions (OmpA-like protein and ABC transporter-related protein), and nucleotide metabolism (HIT family hydrolase).
Improved cell-free RNA and protein synthesis system.
Church et al., Boston, United States. In Plos One, 2013
In this study, using firefly luciferase synthesis as a reporter system, we improved PURE system productivity up to 5 fold by adding or adjusting a variety of factors that affect transcription and translation, including Elongation factors (EF-Ts, EF-Tu, EF-G, and EF4), ribosome recycling factor (RRF), release factors (RF1, RF2, RF3), chaperones (GroEL/ES), BSA and tRNAs.
Molecular insights into replication initiation by Qβ replicase using ribosomal protein S1.
Tomita et al., Tsukuba, Japan. In Nucleic Acids Res, 2013
S1 is also one of the three essential host-derived subunits of Qβ replicase, together with EF-Tu and EF-Ts, for Qβ RNA replication in E. coli.
Structures and functions of Qβ replicase: translation factors beyond protein synthesis.
Tomita, Tsukuba, Japan. In Int J Mol Sci, 2013
Qβ replicase is a unique RNA polymerase complex, comprising Qβ virus-encoded RNA-dependent RNA polymerase (the catalytic β-subunit) and three host-derived factors: translational elongation factor (EF) -Tu, EF-Ts and ribosomal protein S1.
Mutation in the mitochondrial translation elongation factor EFTs results in severe infantile liver failure.
Rötig et al., Paris, France. In J Hepatol, 2012
identified a homozygous mutation changing a highly conserved arginine into a tryptophan (R312W) in a kindred with intrauterine growth retardation, neonatal lactic acidosis, liver dysfunction and multiple respiratory chain deficiency in muscle
Analysis of the functional consequences of lethal mutations in mitochondrial translational elongation factors.
Spremulli et al., Tokyo, Japan. In Biochim Biophys Acta, 2010
Loss of activity is caused by a significant reduction in the ability of EF-Ts(mt) R325W to bind EF-Tu(mt), leading to a defect in nucleotide exchange.
Distinct clinical phenotypes associated with a mutation in the mitochondrial translation elongation factor EFTs.
Shoubridge et al., Nijmegen, Netherlands. In Am J Hum Genet, 2006
Molecular modeling showed that the Arg333Trp substitution disrupts local subdomain structure and the dimerization interface.
Crystal structure of the bovine mitochondrial elongation factor Tu.Ts complex.
Nyborg et al., Århus, Denmark. In J Biol Chem, 2005
X-ray crystallographic structure of the EF-Tumt.Tsmt complex
Isolation, crystallisation, and preliminary X-ray analysis of the bovine mitochondrial EF-Tu:GDP and EF-Tu:EF-Ts complexes.
Clark et al., Århus, Denmark. In Biochim Biophys Acta, 2003
Isolation, crystallisation, and preliminary X-ray analysis
Translational regulation by modifications of the elongation factor Tu.
Kleanthous et al., Leiden, Netherlands. In Folia Microbiol (praha), 1998
Phosphorylation is enhanced by EF-Ts, but inhibited by kirromycin.
Possible evolution of factors involved in protein biosynthesis.
Nyborg, Århus, Denmark. In Acta Biochim Pol, 1997
Elongation factor Ts (EF-Ts) will catalyze the exchange of nucleotide on EF-Tu.
Elongation in bacterial protein biosynthesis.
Kjeldgaard et al., Århus, Denmark. In Curr Opin Biotechnol, 1996
The structures of the ternary complex of aminoacylated tRNA with EF-Tu.GTP and of the complex EF-Tu.EF-Ts have been determined.
The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution.
Leberman et al., Grenoble, France. In Nature, 1996
The crystal structure of the EF-Tu.EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 A. The complex contains two subunits of each of the elongation factors.
Regulatory GTPases.
Hilgenfeld, Jena, Germany. In Curr Opin Struct Biol, 1995
In the field of elongation factors (EFs), three very important structures have been determined: EF-G, the ternary complex of EF-Tu.GTP with aminoacyl-tRNA, and the EF-Tu.EF-Ts complex.
Identification of genes for elongation factor Ts and ribosomal protein S2 in E. coli.
Nomura et al., In Cell, 1976
The structural gene for elongation factor EF-TS (tsf) and that for ribosomal protein S2 (rpsB) have been identified in E. coli.
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