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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Glutamyl-prolyl-tRNA synthetase

glutamyl-prolyl-tRNA synthetase
Top mentioned proteins: ACID, Elongation Factor Tu, p38, Aspartate-tRNA Ligase, CIs
Papers on glutamyl-prolyl-tRNA synthetase
Identification of a gamma interferon-activated inhibitor of translation-like RNA motif at the 3' end of the transmissible gastroenteritis coronavirus genome modulating innate immune response.
Almazán et al., Madrid, Spain. In Mbio, 2014
UNLABELLED: A 32-nucleotide (nt) RNA motif located at the 3' end of the transmissible gastroenteritis coronavirus (TGEV) genome was found to specifically interact with the host proteins glutamyl-prolyl-tRNA synthetase (EPRS) and arginyl-tRNA synthetase (RRS).
Conformational changes in human prolyl-tRNA synthetase upon binding of the substrates proline and ATP and the inhibitor halofuginone.
Hwang et al., Seoul, South Korea. In Acta Crystallogr D Biol Crystallogr, 2013
Halofuginone (HF), a coccidiostat used in veterinary medicine, exerts its effects by acting as a high-affinity inhibitor of the enzyme glutamyl-prolyl-tRNA synthetase (EPRS).
Amino acid-selective segmental isotope labeling of multidomain proteins for structural biology.
Allain et al., Zürich, Switzerland. In Chembiochem, 2013
This approach is illustrated with two multidomain RNA-binding proteins, that is, the two C-terminal RNA-recognition motifs of the human polypyrimidine tract-binding protein, and two highly homologous helix-turn-helix domains of the human glutamyl-prolyl-tRNA synthetase.
Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages.
Fox et al., Cleveland, United States. In Mol Cell Biol, 2012
The gamma interferon (IFN-γ)-activated inhibitor of translation (GAIT) complex in human myeloid cells is heterotetrameric, consisting of glutamyl-prolyl-tRNA synthetase (EPRS), NS1-associated protein 1 (NSAP1), ribosomal protein L13a, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH).
Halofuginone and other febrifugine derivatives inhibit prolyl-tRNA synthetase.
Whitman et al., Boston, United States. In Nat Chem Biol, 2012
Here we show that HF binds glutamyl-prolyl-tRNA synthetase (EPRS), inhibiting prolyl-tRNA synthetase activity; this inhibition is reversed by the addition of exogenous proline or EPRS.
Host cell proteins interacting with the 3' end of TGEV coronavirus genome influence virus replication.
Almazán et al., Madrid, Spain. In Virology, 2009
Gene silencing of PABP, hnRNP Q, and glutamyl-prolyl-tRNA synthetase (EPRS) caused a significant 2 to 3-fold reduction of viral RNA synthesis.
The tumor antigen repertoire identified in tumor-bearing neu transgenic mice predicts human tumor antigens.
Disis et al., Seattle, United States. In Cancer Res, 2006
After screening 3 x 10(6) clones from 3 different cDNA libraries, 15 tumor antigens were identified, including cytokeratin 2-8, glutamyl-prolyl-tRNA synthetase, complement C3, galectin 8, and serine/threonine-rich protein kinase 1.
Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation.
Impact
Fox et al., Cleveland, United States. In Cell, 2004
Here, we show that glutamyl-prolyl-tRNA synthetase (GluProRS), a bifunctional ARS of the MSC, has a regulated, noncanonical activity that blocks synthesis of a specific protein.
The appended C-domain of human methionyl-tRNA synthetase has a tRNA-sequestering function.
Mirande et al., Gif-sur-Yvette, France. In Biochemistry, 2001
It comprises a helix-turn-helix (HTH) motif related to the repeated units of the linker region of bifunctional glutamyl-prolyl-tRNA synthetase, and a specific C-terminal KGKKKK lysine-rich cluster (LRC).
Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats.
Kim et al., Seoul, South Korea. In Biochemistry, 2001
Human bifunctional glutamyl-prolyl-tRNA synthetase (EPRS) contains three tandem repeats linking the two catalytic domains.
Macromolecular assemblage of aminoacyl-tRNA synthetases: quantitative analysis of protein-protein interactions and mechanism of complex assembly.
Mirande et al., Gif-sur-Yvette, France. In J Mol Biol, 2001
This macromolecular assemblage comprises the bifunctional glutamyl-prolyl-tRNA synthetase, the seven monospecific isoleucyl, leucyl, methionyl, glutaminyl, lysyl, arginyl and aspartyl-tRNA synthetases, and the three auxiliary p43, p38 and p18 proteins.
Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases.
Kim et al., Seoul, South Korea. In J Biol Chem, 2000
Interaction of hsp90 with human glutamyl-prolyl-tRNA synthetase (EPRS) was found by genetic screening, co-immunoprecipitation, and in vitro binding experiments.
A gene fusion event in the evolution of aminoacyl-tRNA synthetases.
Mirande et al., Gif-sur-Yvette, France. In Febs Lett, 2000
Our analysis of the extant motifs suggests a possible series of events responsible for a gene fusion that gave rise to the bifunctional glutamyl-prolyl-tRNA synthetase through recombination between genomic sequences encoding the repeated units.
A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases.
Mirande et al., Gif-sur-Yvette, France. In Embo J, 2000
Here we showed by gel retardation and filter binding experiments that the repeated units that build the linker region of the bifunctional glutamyl-prolyl-tRNA synthetase had a general RNA-binding capacity.
Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein.
Mirande et al., Gif-sur-Yvette, France. In J Mol Biol, 1999
This ubiquitous multiprotein assemblage comprises a unique bifunctional aminoacyl-tRNA synthetase, glutamyl-prolyl-tRNA synthetase, as well as the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases.
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