Biosynthesis of Pseudouridine in Transfer Ribonucleic Acid

Cortese, Riccardo; Kammen, Harold O.; Spengler, Sylvia J.; Ames, Bruce N.

doi:10.1016/s0021-9258(19)42947-5

Cited by 141 publications

(24 citation statements)

References 30 publications

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“…A second category consisted of genes with roles in tRNA metabolism (Figure S1B). Insertions in truA, which encodes the pseudouridine synthase that modifies uridines at positions 38, 39, and 40 in the anticodon arm of some tRNAs (Cortese et al, 1974), activate the operon, as do insertions in pnp, which encodes the PNPase exoribonuclease. In E. coli, PNPase degrades aberrant pre-tRNAs (Li et al, 2002).…”

Section: Identification Of Mutations That Results In Operon Activationmentioning

confidence: 99%

An RNA Repair Operon Regulated by Damaged tRNAs

et al. 2020

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Section: Identification Of Mutations That Results In Operon Activationmentioning

confidence: 99%

An RNA Repair Operon Regulated by Damaged tRNAs

et al. 2020

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“…Formally, the extra anticodon loop nucleotide to these suppressors since Bossi et al (1983) showed that mutating the hisT gene, encoding the enzyme that must promote this interaction since it is the only differcatalyzes formation of pseudouridine () at positions ence between the suppressor tRNA and the wild type 38-40 of tRNAs (Cortese et al, 1974), increased the sufJthat cannot suppress, though it could pair in the same mediated suppression. However, the tRNA encoded by way.…”

Section: Discussionmentioning

confidence: 99%

A New Model for Phenotypic Suppression of Frameshift Mutations by Mutant tRNAs

et al. 1998

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According to the prevailing model, frameshift-suppressing tRNAs with an extra nucleotide in the anticodon loop suppress +1 frameshift mutations by recognizing a four-base codon and promoting quadruplet translocation. We present three sets of experiments that suggest a general alternative to this model. First, base modification should actually block such a four-base interaction by two classical frameshift suppressors. Second, for one Salmonella suppressor tRNA, it is not mutant tRNA but a structurally normal near cognate that causes the +1 shift in-frame. Finally, frameshifting occurs in competition with normal decoding of the next in-frame codon, consistent with an event that occurs in the ribosomal P site after the translocation step. These results suggest an alternative model involving peptidyl-tRNA slippage at the classical CCC-N and GGG-N frameshift suppression sites.

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“…The most thoroughly characterized of these variants is the hisT group, which is known to contain a lesion in the structural gene for the enzyme pseudouridylate synthetase, which catalyzes the conversion of specific uridine residues to pseudouridine during maturation of some tRNA's. This function was established by sequence analysis of tRNAHiS isolated from the wild type and from hisT strains of S. typhimurium ( 17) and by the in vitro conversion of uridine to pseudouridine in hisT tRNA by extracts prepared from wild-type cells (7). The hisT mutation is of particular interest because it leads to alterations in tRNA's that contain pseudouridine residues in their anticodon loop.…”

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confidence: 99%