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Cell-free translation reconstituted with purified components
A protein-synthesizing system reconstituted from recombinant tagged protein factors purified to homogeneity was developed, and omission of a release factor allowed efficient incorporation of an unnatural amino acid using suppressor transfer RNA (tRNA).
Human Mitochondrial mRNAs Are Stabilized with Polyadenylation Regulated by Mitochondria-specific Poly(A) Polymerase and Polynucleotide Phosphorylase*
The results demonstrate that the poly(A) length of human mt mRNAs is controlled by polyadenylation by hmtPAP and deadenylations by hPNPase, and polyadenyation is required for the stability of mt m RNAs.
Protein synthesis by pure translation systems.
Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins
- Tatsuya Niwa, Bei-Wen Ying, H. Taguchi
- BiologyProceedings of the National Academy of Sciences
- 17 March 2009
This work individually synthesized the entire ensemble of Escherichia coli proteins by using an in vitro reconstituted translation system and analyzed the aggregation propensities, revealing a clear bimodal distribution and suggesting that the aggregationpropensities are not evenly distributed across a continuum.
Structural basis for template-independent RNA polymerization
The crystal structure of Aquifex aeolicus CCA-adding enzyme represents the ‘pre-insertion’ stage of selecting the incoming nucleotide and provides the structural basis for the mechanism underlying template-independent RNA polymerization.
Evolution of pulmonate gastropod mitochondrial genomes: comparisons of gene organizations of Euhadra, Cepaea and Albinaria and implications of unusual tRNA secondary structures.
The acceptor stems of many tRNAs show a considerable number of mismatched basepairs, indicating that the RNA editing process recently demonstrated in Euhadra is widespread in the pulmonate gastropods.
The 'polysemous' codon--a codon with multiple amino acid assignment caused by dual specificity of tRNA identity.
These findings provide the first evidence that two distinct amino acids are assigned by a single codon, which occurs naturally in the translation process of certain Candida species, and are term this novel type of codon a ‘polysemous codon’.
A cytotoxic ribonuclease targeting specific transfer RNA anticodons.
- T. Ogawa, K. Tomita, T. Ueda, K. Watanabe, T. Uozumi, H. Masaki
- Biology, ChemistryScience
- 26 March 1999
Tight correlation was observed between the toxicity of E5 and the cleavage of intracellular tRNAs of this group, implying that these t RNAs are the primary targets of colicin E5.
Modification Defect at Anticodon Wobble Nucleotide of Mitochondrial tRNAsLeu(UUR) with Pathogenic Mutations of Mitochondrial Myopathy, Encephalopathy, Lactic Acidosis, and Stroke-like Episodes*
- T. Yasukawa, Tsutomu Suzuki, Takeo Suzuki, T. Ueda, S. Ohta, Kimitsuna Watanabe
- BiologyThe Journal of Biological Chemistry
- 11 February 2000
Both of the mutant tRNA molecules were deficient in a modification of uridine that occurs in the normal tRNALeu(UUR) at the first position of the anticodon, which may lead to the mistranslation of leucine into non-cognate phenylalanine codons by mutant tRNAsLeu(U UR), according to the mitochondrial wobble rule, and a decrease in the rate of mitochondrial protein synthesis.
Crystal structures of leucyl/phenylalanyl‐tRNA‐protein transferase and its complex with an aminoacyl‐tRNA analog
Eubacterial leucyl/phenylalanyl‐tRNA protein transferase (L/F‐transferase), encoded by the aat gene, conjugates leucine or phenylalanine to the N‐terminal Arg or Lys residue of proteins, using…