Yeast phenylalanyl-tRNA synthetase: Isolation of subunits on organomercurial-sepharose columns
نویسندگان
چکیده
منابع مشابه
Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase.
Phenylalanyl-tRNA synthetases [L-phenylalanine:tRNAPhe ligase (AMP-forming), EC 6.1.1.20] from Escherichia coli, yeast cytoplasm, and mammalian cytoplasm have an unusual conserved alpha 2 beta 2 quaternary structure that is shared by only one other aminoacyl-tRNA synthetase. Both subunits are required for activity. We show here that a single mitochondrial polypeptide from Saccharomyces cerevisi...
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Next-generation sequencing has turned out to be a powerful tool to uncover genetic basis of childhood mitochondrial disorders. We utilized whole-exome analysis and discovered novel compound heterozygous mutations in FARS2 (mitochondrial phenylalanyl transfer RNA synthetase), encoding the mitochondrial phenylalanyl transfer RNA (tRNA) synthetase (mtPheRS) in two patients with fatal epileptic mit...
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The structural genes for threonyl-tRNA synthetase (ThrRS) and phenylalanyl-tRNA synthetase (PheRS) are closely linked on the Escherichia coli chromosome. To study whether these enzymes share a common regulatory element, we have investigated their synthesis in mutants which were selected for overproduction of either ThrRS or PheRS. It was found that mutants isolated previously for overproduction...
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Plasmid pB1 carries the genes for threonyl-tRNA synthetase, phenylalanyl-tRNA synthetase, and translation initiation factor IF3. Strains carrying this plasmid overproduce phenylalanyl-tRNA synthetase about 100-fold. Spontaneous mutant plasmids were obtained which no longer caused the overproduction of the enzyme. Three classes of mutations were found. (i) Deletion mutations were found, some of ...
متن کاملSite-specific Incorporation of Amino Acid Analogs into Proteins In Vivo by an Engineered Yeast Phenylalanyl-tRNA Synthetase
Aminoacyl-tRNA synthetases (aaRSs) catalyze aminoacylation and establish the rules of genetic code. Precise manipulation of synthetase activity can alter the aminoacylation specificity to attach non-canonical amino acids to the intended transfer RNA (tRNA). Subsequently by codon-anticodon interaction between messenger RNA (mRNA) and tRNA the amino acid analogs can be assigned to specific sites ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1975
ISSN: 0014-5793
DOI: 10.1016/0014-5793(75)80672-7