Nucleotide Sequence of Isoleucine Transfer RNA from Torulopsis utilis

Takemura, Shosuke; Murakami, Mitsukiyo; Miyazaki, Motoichi

doi:10.1093/oxfordjournals.jbchem.a129040

Cited by 48 publications

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“…The investigations centered on the determination of the variation with temperature of the partial specific heat capacities of the tRNA solutions by direct scanning microcalorimetry [16,17]. These quantities sensitively reflect the complex energetics of thermal unfolding and allow calculation of all relevant thermodynamic parameters.…”

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confidence: 99%

Calorimetric Investigations on Thermal Stability of tRNAIle (Yeast) and tRNASer (Yeast)

Filimonov¹,

Privalov²,

Hinz

et al. 1976

Eur J Biochem

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Variation with temperature of the partial heat capacities of tRNAIle (yeast) and tRNASer (yeast) has been determined in two buffers at various salt conditions by scanning microcalorimetry. The overall molar transition enthalpy, ΔHt= 320 ± 20 kcal mol−1 (1339 ± 84 kJ mol−1) is identical for the two tRNA species within the limits of experimental error. ΔHt does not show any dependence on the nature of the buffer, nor does' it vary on addition of 1 mM MgCl2 or 150 mM NaCl. Thermal unfolding of the native structure to the random coil cannot adequately be described by a two‐state, concerted transition under the experimental conditions applied in this study, but exhibits a multistep mechanism characterized by sequential unfolding of separable cooperative domains.

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confidence: 99%

Calorimetric Investigations on Thermal Stability of tRNAIle (Yeast) and tRNASer (Yeast)

Filimonov¹,

Privalov²,

Hinz

et al. 1976

Eur J Biochem

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“…T r a n s f e r RNAS whose codons have a 5'-adenosine usually bear in the position adjacent to the 3'-uridine of the anticodon an unusual nucleoside containing a threonine residue (Takemura et al, 1969;Ishikura et al, 1969;Kimura-Harada et al, 1972a;Powers and Peterkofsky, 1972b). The zyme was purified from E. coli extracts.…”

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confidence: 99%

Enzymic synthesis of N-(purin-6-ylcarbamoyl)threonine, an anticodon-adjacent base in transfer ribonucleic acid

Elkins¹,

Keller²

1974

Biochemistry

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Almost all Escherichia coli tRNAs which have codons with a 5'-adenosine have an unusual nucleoside adjacent to the 3' end of the anticodon the systematic name of which is N -[N-(9-@-D-ribofuranosylpurin-6-yl)carbamoyllthreonine (@A). An enzyme has been isolated from E. coli which can synthesize this nucleoside in t R N A when provided with a t R N A deficient in t6A and with L-threonine, bicarbonate, ATP, and Mg2+. The t6A-deficient tRNA was isolated from a threonine-starved culture of an E. coli strain which is a threonine auxotroph and is also a relaxed control mutant (capable of synthesizing R N A in the absence of protein synthesis). The t6A-deficient t R N A was treated with periodate to destroy the 3'-ribose so that the enzyme assay could depend upon the incorporation of labeled L-threonine into the t R N A to form t6A without interference by the threonine incorporating activity of the E . coli threonyl-tRNA synthetase. Using this assay, an en-

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“…One of the most complex modifications is the N 6 -threonyl-carbamoyl adenosine (t 6 A) is found exclusively at position 37 (3 ′ adjacent to anticodon) of tRNAs that decode codons of the type ANN (where N = A, U, G, or C) ( Fig. 1A; Chheda et al 1969;Takemura et al 1969;Powers and Peterkofsky 1972). Except in some insect symbionts with highly reduced genomes, the t 6 A modification is ubiquitously distributed among cellular organisms as well as in organelles such as mitochondria and chloroplasts (Machnicka et al 2013;Boccaletto et al 2018).…”

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Structure–function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t⁶A tRNA modification

Pichard-Kostuch

Zhang

Liger

et al. 2018

RNA

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-threonyl-carbamoyl adenosine (tA) is a universal tRNA modification found at position 37, next to the anticodon, in almost all tRNAs decoding ANN codons (where N = A, U, G, or C). tA stabilizes the codon-anticodon interaction and hence promotes translation fidelity. The first step of the biosynthesis of tA, the production of threonyl-carbamoyl adenylate (TC-AMP), is catalyzed by the Sua5/TsaC family of enzymes. While TsaC is a single domain protein, Sua5 enzymes are composed of the TsaC-like domain, a linker and an extra domain called SUA5 of unknown function. In the present study, we report structure-function analysis of Sua5 (-Sua5). Crystallographic data revealed binding sites for bicarbonate substrate and pyrophosphate product. The linker of -Sua5 forms a loop structure that folds into the active site gorge and closes it. Using structure-guided mutational analysis, we established that the conserved sequence motifs in the linker and the domain-domain interface are essential for the function of-Sua5. We propose that the linker participates actively in the biosynthesis of TC-AMP by binding to ATP/PPi and by stabilizing the -carboxy-l-threonine intermediate. Hence, TsaC orthologs which lack such a linkerand SUA5 domain use a different mechanism for TC-AMP synthesis.

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Nucleotide Sequence of Isoleucine Transfer RNA from Torulopsis utilis

Cited by 48 publications

References 0 publications

Calorimetric Investigations on Thermal Stability of tRNAIle (Yeast) and tRNASer (Yeast)

Calorimetric Investigations on Thermal Stability of tRNAIle (Yeast) and tRNASer (Yeast)

Enzymic synthesis of N-(purin-6-ylcarbamoyl)threonine, an anticodon-adjacent base in transfer ribonucleic acid

Structure–function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t⁶A tRNA modification

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Nucleotide Sequence of Isoleucine Transfer RNA from Torulopsis utilis

Cited by 48 publications

References 0 publications

Calorimetric Investigations on Thermal Stability of tRNAIle (Yeast) and tRNASer (Yeast)

Calorimetric Investigations on Thermal Stability of tRNAIle (Yeast) and tRNASer (Yeast)

Enzymic synthesis of N-(purin-6-ylcarbamoyl)threonine, an anticodon-adjacent base in transfer ribonucleic acid

Structure–function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t6A tRNA modification

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Resources

About

Structure–function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t⁶A tRNA modification