The m1A58 modification in eubacterial tRNA: An overview of tRNA recognition and mechanism of catalysis by TrmI

Dégut, Clément; Ponchon, Luc; Folly-Klan, Marcia; Barraud, Pierre; Tisné, Carine

doi:10.1016/j.bpc.2015.06.012

Cited by 22 publications

(19 citation statements)

References 64 publications

(98 reference statements)

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“…Due to the differences in protonation states of the N1 atom at physiological pH, the formation of m 1 A must proceed via a mechanism different from m 1 G. Two mechanisms for formation of m 1 A have been proposed, based on investigations on the m 1 A58 specific RFM family member TrmI from the eubacteria T. thermophilus [65,66]. In the first mechanism (Figure 4B), a deprotonation takes place as the initial step.…”

Section: Mechanism For Formation Of the N1-methylation In Trnamentioning

confidence: 99%

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m1A Post‐Transcriptional Modification in tRNAs

et al. 2017

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To date, about 90 post-transcriptional modifications have been reported in tRNA expanding their chemical and functional diversity. Methylation is the most frequent post-transcriptional tRNA modification that can occur on almost all nitrogen sites of the nucleobases, on the C5 atom of pyrimidines, on the C2 and C8 atoms of adenosine and, additionally, on the oxygen of the ribose 2′-OH. The methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. This review provides an overview of the currently known m1A modifications, the different m1A modification sites, the biological role of each modification, and the enzyme responsible for each methylation in different species. The review further describes, in detail, two enzyme families responsible for formation of m1A at nucleotide position 9 and 58 in tRNA with a focus on the tRNA binding, m1A mechanism, protein domain organisation and overall structures.

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Section: Mechanism For Formation Of the N1-methylation In Trnamentioning

confidence: 99%

“…A structure of the human complex bound to tRNA is also reported [67]. Structures of homotetrameric TrmI proteins are available for the archaea Pyrococcus abyssi [73], and the bacteria T. thermophilus [65,66], Aquifex aeolicus [74], Thermotoga maritima (Joint Center for Structural Genomics 2003, PDB 1O54), and Mycobacterium tuberculosis [75]. …”

Section: M1a58mentioning

confidence: 99%

m1A Post‐Transcriptional Modification in tRNAs

et al. 2017

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“…Taken together, it has been proposed a hypothetical mechanism for TrmB in which the carboxyl group of Asp133 captures the proton of N–H of the guanine base and the N7 atom of the guanine base itself attacks the methyl group in AdoMet [25] (Figure 4B). A hypothetical catalytic mechanism for TrmI, which is a methyltransferase for the N1 atom of adenosine at position 58 in tRNA, has also been proposed [62]. In this mechanism, the N1 atom causes a nucleophilic attack on the methyl group of AdoMet.…”

Section: Structural Analyses and Catalytic Mechanisms Of M7g Methymentioning

confidence: 99%

7-Methylguanosine Modifications in Transfer RNA (tRNA)

Tomikawa

2018

IJMS

171

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More than 90 different modified nucleosides have been identified in tRNA. Among the tRNA modifications, the 7-methylguanosine (m7G) modification is found widely in eubacteria, eukaryotes, and a few archaea. In most cases, the m7G modification occurs at position 46 in the variable region and is a product of tRNA (m7G46) methyltransferase. The m7G46 modification forms a tertiary base pair with C13-G22, and stabilizes the tRNA structure. A reaction mechanism for eubacterial tRNA m7G methyltransferase has been proposed based on the results of biochemical, bioinformatic, and structural studies. However, an experimentally determined mechanism of methyl-transfer remains to be ascertained. The physiological functions of m7G46 in tRNA have started to be determined over the past decade. For example, tRNA m7G46 or tRNA (m7G46) methyltransferase controls the amount of other tRNA modifications in thermophilic bacteria, contributes to the pathogenic infectivity, and is also associated with several diseases. In this review, information of tRNA m7G modifications and tRNA m7G methyltransferases is summarized and the differences in reaction mechanism between tRNA m7G methyltransferase and rRNA or mRNA m7G methylation enzyme are discussed.

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“…TRMT61B is a dual function methyltransferase that modifies both mt-tRNA (Chujo and Suzuki, 2012) and mt-rRNA (Bar-Yaacov et al, 2016). The conserved residues of its bacterial homolog, TrmI, are well characterized for their catalytic function (Barraud et al, 2008) and contribution to binding of SAM (Dégut et al, 2016). TrmI is responsible for SAM-dependent N 1 -methylation of adenosine 58 in the T-loop of many tRNAs and its inactivation in the hyperthermophilic bacterium T. thermophilus results in a thermosensitive phenotype (Droogmans et al, 2003).…”

Section: Trmt61b (M 1 A947)mentioning

confidence: 99%

Methylation of Ribosomal RNA: A Mitochondrial Perspective

et al. 2020

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Ribosomal RNA (rRNA) from all organisms undergoes post-transcriptional modifications that increase the diversity of its composition and activity. In mitochondria, specialized mitochondrial ribosomes (mitoribosomes) are responsible for the synthesis of 13 oxidative phosphorylation proteins encoded by the mitochondrial genome. Mitoribosomal RNA is also modified, with 10 modifications thus far identified and all corresponding modifying enzymes described. This form of epigenetic regulation of mitochondrial gene expression affects mitoribosome biogenesis and function. Here, we provide an overview on rRNA methylation and highlight critical work that is beginning to elucidate its role in mitochondrial gene expression. Given the similarities between bacterial and mitochondrial ribosomes, we focus on studies involving Escherichia coli and human models. Furthermore, we highlight the use of state-of-the-art technologies, such as cryoEM in the study of rRNA methylation and its biological relevance. Understanding the mechanisms and functional relevance of this process represents an exciting frontier in the RNA biology and mitochondrial fields.

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The m1A58 modification in eubacterial tRNA: An overview of tRNA recognition and mechanism of catalysis by TrmI

Cited by 22 publications

References 64 publications

m1A Post‐Transcriptional Modification in tRNAs

m1A Post‐Transcriptional Modification in tRNAs

7-Methylguanosine Modifications in Transfer RNA (tRNA)

Methylation of Ribosomal RNA: A Mitochondrial Perspective

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