Biosynthesis and specific labeling of N-(purin-6-ylcarbamoyl)threonine of Escherichiacoli transfer RNA

Powers, Donald M.; Peterkofsky, Alan

doi:10.1016/s0006-291x(72)80216-x

Cited by 36 publications

(24 citation statements)

References 10 publications

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“…The biosynthesis of t 6 A 37 utilizes free threonine from the cell as the threonyl-moiety for production of the threonylcarbamoyl (Powers and Peterkofsky 1972). If YrdC is involved in the enzymatic pathway, it could potentially bind threonine, ATP, and/or the carboxylphosphate.…”

Section: Yrdc Recognizes Threonine and Atpmentioning

confidence: 99%

“…The reaction requires ATP, free threonine, and a single carbon source (Chheda et al 1972;Powers and Peterkofsky 1972;Elkins and Keller 1974;Körner and Söll 1974). Studies of t 6 A biosynthesis in vitro have demonstrated that Escherichia coli extracts contain an enzymatic component required for synthesis, but the identity of that enzyme remains unknown (Elkins and Keller 1974;Körner and Söll 1974).…”

Section: Introductionmentioning

confidence: 99%

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YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase

Harris¹,

Jones²,

Bilbille³

et al. 2011

RNA

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The post-transcriptional nucleoside modifications of tRNA's anticodon domain form the loop structure and dynamics required for effective and accurate recognition of synonymous codons. The N 6 -threonylcarbamoyladenosine modification at position 37 (t 6 A 37 ), 39-adjacent to the anticodon, of many tRNA species in all organisms ensures the accurate recognition of ANN codons by increasing codon affinity, enhancing ribosome binding, and maintaining the reading frame. However, biosynthesis of this complex modification is only partially understood. The synthesis requires ATP, free threonine, a single carbon source for the carbamoyl, and an enzyme yet to be identified. Recently, the universal protein family Sua5/YciO/YrdC was associated with t . YrdC also demonstrated specificity toward the unmodified versus modified anticodon pentamer UUUUA and toward threonine and ATP. The protein did not significantly alter the ASL architecture, nor was it able to base flip A 37 , as determined by NMR, circular dichroism, and fluorescence of 2-aminopuine at position 37. Thus, current data support the hypothesis that YrdC, with many of the properties of a putative threonylcarbamoyl transferase, most likely functions as a component of a heteromultimeric protein complex for t 6 A 37 biosynthesis.

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Section: Yrdc Recognizes Threonine and Atpmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase

Harris¹,

Jones²,

Bilbille³

et al. 2011

RNA

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show abstract

“…12 The hypermodified base t 6 A is present in nearly all ANN decoding tRNAs and has been studied in vitro and in vivo for more than 40 y. [13][14][15][16][17][18][19] Since the first discovery of the modification by Schweizer, et al in 1969, 18 sporadic studies established the basic requirements for the synthesis of this universal modification, identifying the requirement for ATP, threonine and carbonate, 15,17,[20][21][22] but fell short of elucidating the multi-step path to its formation. Subsequent studies in which native E. coli tRNA fMet (harboring an unmodified A 37 ) and yeast tRNA iMet transcripts were converted to t 6 A 37 after microinjection into Xenopus laevis oocytes demonstrated that the formation of t 6 A occurred in the oocyte cytoplasm and used a conserved machinery.…”

mentioning

confidence: 99%

Diversity of the biosynthesis pathway for threonylcarbamoyladenosine (t⁶A), a universal modification of tRNA

2014

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“…The following experiment was carried out to determine whether the tRNA of R. roseolus contained Ado-CO-thr. Radioactive threonine has been incorporated into the Ado-CO-thr residues of tRNA of E. coli (18) and rat liver (7). We used both radioactive threonine and adenine as precursors.…”

Section: Incorporation Of Radioactive Labeled Threonine Andmentioning

confidence: 99%

“…The threonine-containing side chain of the Ado-CO-thr residues in tRNA appears to be attached at the macromolecular level (7,18) LITERATURE CITED…”

Section: Incorporation Of Radioactive Labeled Threonine Andmentioning

confidence: 99%

Cytokinins in Rhizopogon roseolus Secretion of N-[9-(β-d-Ribofuranosyl-9H) Purin-6-Ylcarbamoyl]Threonine into the Culture Medium

Laloue

Hall²

1973

Plant Physiol.

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Biosynthesis and specific labeling of N-(purin-6-ylcarbamoyl)threonine of Escherichiacoli transfer RNA

Cited by 36 publications

References 10 publications

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase

Diversity of the biosynthesis pathway for threonylcarbamoyladenosine (t⁶A), a universal modification of tRNA

Cytokinins in Rhizopogon roseolus Secretion of N-[9-(β-d-Ribofuranosyl-9H) Purin-6-Ylcarbamoyl]Threonine into the Culture Medium

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Biosynthesis and specific labeling of N-(purin-6-ylcarbamoyl)threonine of Escherichiacoli transfer RNA

Cited by 36 publications

References 10 publications

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase

YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase

Diversity of the biosynthesis pathway for threonylcarbamoyladenosine (t6A), a universal modification of tRNA

Cytokinins in Rhizopogon roseolus Secretion of N-[9-(β-d-Ribofuranosyl-9H) Purin-6-Ylcarbamoyl]Threonine into the Culture Medium

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Diversity of the biosynthesis pathway for threonylcarbamoyladenosine (t⁶A), a universal modification of tRNA