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Phenylalanyl-tRNA synthetase 2, mitochondrial

Phenylalanine-tRNA Ligase, phenylalanyl-tRNA synthetase, PheRS
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. This gene encodes a phenylalanine-tRNA synthetase (PheRS) localized to the mitochondrion which consists of a single polypeptide chain, unlike the (alpha-beta)2 structure of the prokaryotic and eukaryotic cytoplasmic forms of PheRS. Structure analysis and catalytic properties indicate mitochondrial PheRSs may constitute a class of PheRS distinct from the enzymes found in prokaryotes and in the eukaryotic cytoplasm. [provided by RefSeq, Jul 2008] (from NCBI)
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Papers on Phenylalanine-tRNA Ligase
Rationally evolving tRNAPyl for efficient incorporation of noncanonical amino acids.
Söll et al., New Haven, United States. In Nucleic Acids Res, Jan 2016
This improved tRNA was tested as substrate for wild-type PylRS as well as three characterized PylRS variants (N(ϵ)-acetyllysyl-tRNA synthetase [AcKRS], 3-iodo-phenylalanyl-tRNA synthetase [IFRS], a broad specific PylRS variant [PylRS-AA]) to incorporate ncAAs at UAG codons in super-folder green fluorescence protein (sfGFP).
Chimeric human mitochondrial PheRS exhibits editing activity to discriminate non-protein amino acids.
Safro et al., Israel. In Protein Sci, Jan 2016
Phenylalanine exposure to ROS produces multiple oxidized isomers: tyrosine, Levodopa, ortho-Tyr, meta-Tyr (m-Tyr) etc. Cytosolic phenylalanyl-tRNA synthetase (PheRS) exerts control over the translation accuracy, hydrolyzing misacylated products, while monomeric mitochondrial PheRS lacks the editing activity.
Lactobacillus herbarum sp. nov., a species related to Lactobacillus plantarum.
Horvath et al., Shanghai, China. In Int J Syst Evol Microbiol, Dec 2015
pheS (phenylalanyl-tRNA synthetase alpha subunit) and 89.5-94.9%
Efficient Reassignment of a Frequent Serine Codon in Wild-Type Escherichia coli.
Söll et al., Boston, United States. In Acs Synth Biol, Dec 2015
Our results indicate that the 3-iodo-l-phenylalanyl-tRNA synthetase (IFRS)/tRNA(Pyl) pair can efficiently outcompete the cellular machinery to reassign select sense codons in wild-type E. coli.
A novel therapeutic target for peripheral nerve injury-related diseases: aminoacyl-tRNA synthetases.
Jeong et al., Seoul, South Korea. In Neural Regen Res, Oct 2015
Of 20 AminoARSs, we found that phenylalanyl-tRNA synthetase beta chain (FARSB), isoleucyl-tRNA synthetase (IARS) and methionyl-tRNA synthetase (MARS) mRNA expression was increased in spinal dorsal horn neurons on the injured side, but not in glial cells.
Probiotic attributes of Lactobacillus fermentum isolated from human feces and dairy products.
Halami et al., Mysore, India. In Appl Microbiol Biotechnol, Oct 2015
Molecular fingerprinting and identification of the isolates were achieved by PCR with GTG5 as well as 16S rRNA, phenylalanyl-tRNA synthetase alpha subunit (pheS), and RNA polymerase alpha subunit (rpoA) genes.
Mutations in FARS2 and non-fatal mitochondrial dysfunction in two siblings.
Naidu et al., Baltimore, United States. In Am J Med Genet A, May 2015
Recently, mutations in FARS2, which encodes for mitochondrial phenylalanyl-tRNA synthetase, have been implicated in autosomal recessive combined oxidative phosphorylation deficiency 14.
Universal pathway for posttransfer editing reactions: insights from the crystal structure of TtPheRS with puromycin.
Safro et al., Israel. In Proc Natl Acad Sci U S A, May 2015
At the amino acid binding and recognition step, phenylalanyl-tRNA synthetase (PheRS) faces the challenge of discrimination between cognate phenylalanine and closely similar noncognate tyrosine.
Click Grafting of Alkyne-containing Vinyl Polymers onto Biosynthesized Extracellular Matrix Protein Containing Azide Functionality and Adhesion Control of Human Umbilical Vein Endothelial Cells.
Takasu et al., Nagoya, Japan. In Rsc Adv, 2015
UNASSIGNED: In vivo incorporation of a phenylalanine (Phe) analogue, p-azidophenylalanine (p-N3Phe) into an artificial extracellular matrix protein (aECM-CS5-ELF) was accomplished using a bacterial expression host that harbors the mutant phenylalanyl-tRNA synthetase (PheRS) with an enlarged binding pocket, in which the Ala294Gly/Thr251Gly mutant PheRS (PheRS**) was expressed under the control of T7 promoters.
Aminoacyl-tRNA synthetase inhibitors as potent antibacterials.
Zhu et al., Nanjing, China. In Curr Med Chem, 2011
In this review, we examine the latest developments and structure-activity relationship (SAR) analysis of aminoacyl-tRNA synthetases inhibitors, including methionyl-tRNA synthetase, isoleucyl-tRNA synthetase and phenylalanyl-tRNA synthetase inhibitors.
Mitochondrial aminoacyl-tRNA synthetase single-nucleotide polymorphisms that lead to defects in refolding but not aminoacylation.
Ibba et al., Columbus, United States. In J Mol Biol, 2011
Two phenylalanyl-tRNA synthetase variants Ser57Cys and Asp280Ser both display wild-type aminoacylation activity and stability with respect to their free energies of unfolding, but are less stable at low hydrogen-ion concentration (pH).
Large-scale movement of functional domains facilitates aminoacylation by human mitochondrial phenylalanyl-tRNA synthetase.
Ibba et al., Columbus, United States. In Febs Lett, 2009
these results indicate that conformational flexibility of the two functional modules in mtPheRS is essential for its phenylalanylation activity.
Eukaryotic cytosolic and mitochondrial phenylalanyl-tRNA synthetases catalyze the charging of tRNA with the meta-tyrosine.
Safro et al., Israel. In Proc Natl Acad Sci U S A, 2009
Mitochondrial and cytoplasmic phenylalanyl-tRNA synthetases (HsmtPheRS and HsctPheRS, respectively) catalyze direct attachment of m-Tyr to tRNA(Phe).
Crystallization and X-ray analysis of human cytoplasmic phenylalanyl-tRNA synthetase.
Safro et al., Israel. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009
The structure of phenylalanyl-tRNA synthetase was determined to be 3.3 A resolution by x-ray diffraction.
The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase.
Safro et al., Israel. In Structure, 2008
Formation of the PheRS-tRNAPhe complex in human mitochondria must be accompanied by considerable rearrangement of the anticodon binding domain upon tRNA binding.
Molecular signatures (unique proteins and conserved indels) that are specific for the epsilon proteobacteria (Campylobacterales).
Gupta, Hamilton, Canada. In Bmc Genomics, 2005
B subunit of exinuclease ABC, phenylalanyl-tRNA synthetase, RNA polymerase beta '-subunit and FtsH protein) that are specific for either all epsilon proteobacteria or different subgroups.
Genomic and phylogenetic perspectives on the evolution of prokaryotes.
Brown, United States. In Syst Biol, 2001
Here phenylalanyl-tRNA synthetase is used as an example of the complex interplay among lateral gene transfer, operon recombination, and gene recruitment in the evolution of some prokaryotic genes.
Glycyl-tRNA synthetase.
Gauss et al., Göttingen, Germany. In Biol Chem Hoppe Seyler, 1996
The alpha 2 beta 2 enzymes exhibit similarities to PheRS (also an alpha 2 beta 2 enzyme).
Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs.
Moras et al., Strasbourg, France. In Nature, 1990
These three latter aaRS share three new sequence motifs with AspRS, AsnRS, LysRS, HisRS and the beta subunit of PheRS.
Nucleotides in yeast tRNAPhe required for the specific recognition by its cognate synthetase.
Uhlenbeck et al., Boulder, United States. In Science, 1989
An analysis of the aminoacylation kinetics of unmodified yeast tRNAPhe mutants revealed that five single-stranded nucleotides are important for its recognition by yeast phenylalanyl-tRNA synthetase, provided they were positioned correctly in a properly folded tRNA structure.
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