gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Tyrosyl-tRNA synthetase

tyrosyl-tRNA synthetase, Yars
Top mentioned proteins: ACID, CAN, STEP, OUT, fibrillin-1
Papers on tyrosyl-tRNA synthetase
Redesigning the stereospecificity of tyrosyl-tRNA synthetase.
Plateau et al., Palaiseau, France. In Proteins, Feb 2016
Several aaRSs can aminoacylate their tRNA with a d-amino acid; of these, tyrosyl-tRNA synthetase (TyrRS) has the weakest stereospecificity.
Alternative splicing creates two new architectures for human tyrosyl-tRNA synthetase.
Schimmel et al., Hong Kong, Hong Kong. In Nucleic Acids Res, Feb 2016
Here, we report analysis of two closely related, internally deleted, SVs of homodimeric human tyrosyl-tRNA synthetase (TyrRS).
Improved Incorporation of Noncanonical Amino Acids by an Engineered tRNA(Tyr) Suppressor.
Perona et al., Portland, United States. In Biochemistry, Feb 2016
UNASSIGNED: The Methanocaldcoccus jannaschii tyrosyl-tRNA synthetase (TyrRS):tRNA(Tyr) cognate pair has been used to incorporate a large number of noncanonical amino acids (ncAAs) into recombinant proteins in Escherichia coli.
Clinical, neurophysiological and morphological study of dominant intermediate Charcot-Marie-Tooth type C neuropathy.
Jordanova et al., Saint Louis, United States. In J Neurol, Feb 2016
UNASSIGNED: Dominant intermediate Charcot-Marie-Tooth neuropathy subtype C (DI-CMTC) was associated with mutations in the YARS gene, encoding tyrosyl-tRNA synthetase, in two large unrelated Bulgarian and US pedigrees and one sporadic case.
Targeting druggable enzymome by exploiting natural medicines: An in silico-in vitro integrated approach to combating multidrug resistance in bacterial infection.
Yu et al., Weifang, China. In Pharm Biol, Jan 2016
DISCUSSION AND CONCLUSION: Combined quantum mechanics/molecular mechanics analysis revealed diverse non-bonded interactions across the complex interfaces of newly identified antibacterial agents with their putative targets GyrB ATPase and tyrosyl-tRNA synthetase.
Structure of a tyrosyl-tRNA synthetase splicing factor bound to a group I intron RNA.
Golden et al., Austin, United States. In Nature, 2008
One such protein, the Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (TyrRS; CYT-18), is bifunctional and both aminoacylates mitochondrial tRNA(Tyr) and promotes the splicing of mitochondrial group I introns.
Efficient incorporation of unnatural amino acids into proteins in Escherichia coli.
Schultz et al., Los Angeles, United States. In Nat Methods, 2006
In this system, multiple copies of a gene encoding an amber suppressor tRNA derived from a Methanocaldococcus jannaschii tyrosyl-tRNA (MjtRNATyrCUA) are expressed under control of the proK promoter and terminator, and a gene encoding the desired mutant M. jannaschii tyrosyl-tRNA synthetase (MjTyrRS) is expressed under control of a mutant glnS (glnS') promoter.
Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy.
Timmerman et al., Antwerp, Belgium. In Nat Genet, 2006
Here we identify two heterozygous missense mutations (G41R and E196K) and one de novo deletion (153-156delVKQV) in tyrosyl-tRNA synthetase (YARS) in three unrelated families affected with DI-CMTC.
Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid.
Yokoyama et al., Tokyo, Japan. In Nat Methods, 2005
The human GRB2 gene with an amber codon was introduced into Chinese hamster ovary (CHO) cells, together with the genes for the Bacillus stearothermophilus suppressor tRNA(Tyr) and a pBpa-specific variant of Escherichia coli tyrosyl-tRNA synthetase (TyrRS).
Relationship of two human tRNA synthetases used in cell signaling.
Ewalt et al., Los Angeles, United States. In Trends Biochem Sci, 2004
Human tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA synthetase (TrpRS) are closely related, dual function enzymes that act in protein biosynthesis and angiogenesis.
An efficient system for the evolution of aminoacyl-tRNA synthetase specificity.
Schultz et al., Los Angeles, United States. In Nat Biotechnol, 2002
Using this system to explore the evolvability of an amino acid binding pocket of a tyrosyl-tRNA synthetase, we identified three new variants that allow the selective incorporation of amino-, isopropyl-, and allyl-containing tyrosine analogs into a desired protein.
Azatyrosine. Mechanism of action for conversion of transformed phenotype to normal.
Nishimura et al., Tsukuba, Japan. In Ann N Y Acad Sci, 1998
To prove this hypothesis, we are attempting to develop a mutant of tyrosyl-tRNA synthetase that, unlike wild type, can aminoacylate azatyrosine more efficiently than can tyrosine.
Non-canonical substrates of aminoacyl-tRNA synthetases: the tRNA-like structure of brome mosaic virus genomic RNA.
Giegé et al., Strasbourg, France. In Biochimie, 1992
For that, we show how the present structural model rationalises mutagenic and footprinting data that have established the importance of specific regions of the RNA for its recognition and aminoacylation by yeast tyrosyl-tRNA synthetase.
Discrimination between transfer-RNAs by tyrosyl-tRNA synthetase.
Nageotte et al., Paris, France. In Biochimie, 1992
We have constructed a model of the complex between tyrosyl-tRNA synthetase (TyrRS) from Bacillus stearothermophilus and tRNA(Tyr) by successive cycles of predictions, mutagenesis of TyrRS and molecular modeling.
Recognition of tRNA(Tyr) by tyrosyl-tRNA synthetase.
Bedouelle, Paris, France. In Biochimie, 1990
In this review, I have brought together and compared the available data on the interaction between tRNA(Tyr) and tyrosyl-tRNA synthetases (TyrTS) of prokaryotic origins.
share on facebooktweetadd +1mail to friends