Three modified nucleosides present in the anticodon stem and loop influence the in vivo aa-tRNA selection in a tRNA-dependent manner

Li, Ji-nong; Esberg, Birgitta; Curran, James F.; Björk, Glenn R.

doi:10.1006/jmbi.1997.1176

Cited by 83 publications

(99 citation statements)

References 51 publications

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“…Another way is the use of programmed frameshift assays, which allow the determination of the contribution of a modified nucleotide on reading frame maintenance (13,30). These systems have been mainly used in prokaryotes, and only limited data are available for eukaryotic systems.…”

Section: Discussionmentioning

confidence: 99%

“…48). Moreover, it has been shown recently (13,30) that in a bacterial system the presence or absence of certain modified nucleotides within the anticodon loop of tRNA also affect the probability of a frameshift event, possibly by affecting the rate at which the incoming tRNA in the A-site will be recruited by the mRNA-peptidyl-tRNA ribosome complex or by affecting the probability of peptidyl-tRNA slippage in the P-site.…”

Section: Fig 1 Type and Location Of Modified Nucleotides Catalyzed Bymentioning

confidence: 99%

“…However, this phenotype for truB mutant is due to the absence of the protein TruB and not to the absence of ⌿55 per se (12). In truA mutant cells, which are unable to modify the uridines at positions 38, 39, and 40, a decrease in the rate of the aminoacyl-tRNA selection step during translation depending on the identity of the tRNA has been demonstrated (13). This observation could explain the pleiotropic phenotype of truA mutant cells, like derepression of his, leu, and ilv operons, reduction of growth, and polypeptide chain elongation rates (reviewed in Ref.…”

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confidence: 99%

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Lack of Pseudouridine 38/39 in the Anticodon Arm of Yeast Cytoplasmic tRNA Decreases in Vivo Recoding Efficiency

Lecointe¹,

Namy²,

Hatin³

et al. 2002

Journal of Biological Chemistry

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Many different modified nucleotides are found in naturally occurring tRNA, especially in the anticodon region. Their importance for the efficiency of the translational process begins to be well documented. Here we have analyzed the in vivo effect of deleting genes coding for yeast tRNA-modifying enzymes, namely Pus1p, Pus3p, Pus4p, or Trm4p, on termination readthrough and ؉1 frameshift events. To this end, we have transformed each of the yeast deletion strains with a lacZ-luc dual-reporter vector harboring selected programmed recoding sites. We have found that only deletion of the PUS3 gene, encoding the enzyme that introduces pseudouridines at position 38 or 39 in tRNA, has an effect on the efficiency of the translation process. In this mutant, we have observed a reduced readthrough efficiency of each stop codon by natural nonsense suppressor tRNAs. This effect is solely due to the absence of pseudouridine 38 or 39 in tRNA because the inactive mutant protein Pus3[D151A]p did not restore the level of natural readthrough. Our results also show that absence of pseudouridine 39 in the slippery tRNA UAG Leu reduces ؉1 frameshift efficiency. Therefore, the presence of pseudouridine 38 or 39 in the tRNA anticodon arm enhances misreading of certain codons by natural nonsense tRNAs as well as promotes frameshifting on slippery sequences in yeast.

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Section: Discussionmentioning

confidence: 99%

Section: Fig 1 Type and Location Of Modified Nucleotides Catalyzed Bymentioning

confidence: 99%

mentioning

confidence: 99%

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Lack of Pseudouridine 38/39 in the Anticodon Arm of Yeast Cytoplasmic tRNA Decreases in Vivo Recoding Efficiency

Lecointe¹,

Namy²,

Hatin³

et al. 2002

Journal of Biological Chemistry

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“…Characteristically, mutations in miaA cause broad pleiotropic phenotypes, including decreased growth rate and yield, broad changes in the biosynthesis and utilization of certain amino acids, defects in translation efficiency and fidelity (especially of specific regulatory genes), increased susceptibility to antibiotics and reduced virulence [32,54]. For example, cellular yields of miaA mutants in S. enterica sv.…”

Section: Discussionmentioning

confidence: 99%

“…Studies of tRNA modification mutants demonstrate extensive phenotypic consequences due to the disruption of specific tRNA modification enzymes. In miaA mutants, A-37 remains unmodified, leading to deficiencies in tRNAs with ms 2 i 6 A-37 (E. coli) or ms 2 io 6 A-37 (Salmonella typhimurium) and resulting in multiple defects in translation efficiency, codon context sensitivity and fidelity [32]. Several studies have shown that mutation of miaA caused decreased growth rates and yield, and it altered sensitivity to amino acid analogues [33], altered aromatic amino acid biosynthesis and transport [34], altered utilization of primary carbon sources [35] and reduced leu operon expression [36].…”

Section: Introductionmentioning

confidence: 99%

Disruption of MiaA provides insights into the regulation of phenazine biosynthesis under suboptimal growth conditions in Pseudomonas chlororaphis 30-84

Wang

Pierson

et al. 2017

Microbiology

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Many products of secondary metabolism are activated by quorum sensing (QS), yet even at cell densities sufficient for QS, their production may be repressed under suboptimal growth conditions via mechanisms that still require elucidation. For many beneficial plant-associated bacteria, secondary metabolites such as phenazines are important for their competitive survival and plant-protective activities. Previous work established that phenazine biosynthesis in Pseudomonas chlororaphis 30-84 is regulated by the PhzR/PhzI QS system, which in turn is regulated by transcriptional regulator Pip, two-component system RpeA/RpeB and stationary phase/stress sigma factor RpoS. Disruption of MiaA, a tRNA modification enzyme, altered primary metabolism and growth leading to widespread effects on secondary metabolism, including reduced phenazine production and oxidative stress tolerance. Thus, the miaA mutant provided the opportunity to examine the regulation of phenazine production in response to altered metabolism and growth or stress tolerance. Despite the importance of MiaA for translation efficiency, the most significant effect of miaA disruption on phenazine production was the reduction in the transcription of phzR, phzI and pip, whereas neither the transcription nor translation of RpeB, a transcriptional regulator of pip, was affected. Constitutive expression of rpeB or pip in the miaA mutant completely restored phenazine production, but it resulted in further growth impairment. Constitutive expression of RpoS alleviated sensitivity to oxidative stress resulting from RpoS translation inefficiency in the miaA mutant, but it did not restore phenazine production. Our results support the model that cells curtail phenazine biosynthesis under suboptimal growth conditions via RpeB/Pip-mediated regulation of QS.

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A cytosolic tRNA with an unmodified adenosine in the wobble position reads a codon ending with the non-complementary nucleoside cytidine 1 1Edited by D. Draper

Chen

Qian

Zhang

et al. 2002

Journal of Molecular Biology

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Three modified nucleosides present in the anticodon stem and loop influence the in vivo aa-tRNA selection in a tRNA-dependent manner

Cited by 83 publications

References 51 publications

Lack of Pseudouridine 38/39 in the Anticodon Arm of Yeast Cytoplasmic tRNA Decreases in Vivo Recoding Efficiency

Lack of Pseudouridine 38/39 in the Anticodon Arm of Yeast Cytoplasmic tRNA Decreases in Vivo Recoding Efficiency

Disruption of MiaA provides insights into the regulation of phenazine biosynthesis under suboptimal growth conditions in Pseudomonas chlororaphis 30-84

A cytosolic tRNA with an unmodified adenosine in the wobble position reads a codon ending with the non-complementary nucleoside cytidine 1 1Edited by D. Draper

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