Required Elements in tRNA for Methylation by the Eukaryotic tRNA (Guanine-N2-) Methyltransferase (Trm11-Trm112 Complex)

Nishida, Yasuhiro; Ohmori, S.; Kakizono, Risa; Kawai, Kunpei; Namba, Miyu; Okada, Kazuki; Yamagami, Ryota; Hirata, Akira; Hori, Hiroyuki

doi:10.3390/ijms23074046

Cited by 6 publications

(2 citation statements)

References 82 publications

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“…tRNAs specific for Arg, Asn, Ile, Leu, Lys, Met, Phe, Thr, Trp, Tyr and Val). In addition, U 38 in tRNA Ala and the U 32 –A 38 base pair in tRNA Cys are negative identity elements against this methylation ( 401 ). For t 6 A 37 biosynthesis (e.g.…”

Section: Expanding the World Of Trna Identitymentioning

confidence: 99%

The tRNA identity landscape for aminoacylation and beyond

Giegé

Eriani

2023

Nucleic Acids Research

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tRNAs are key partners in ribosome-dependent protein synthesis. This process is highly dependent on the fidelity of tRNA aminoacylation by aminoacyl-tRNA synthetases and relies primarily on sets of identities within tRNA molecules composed of determinants and antideterminants preventing mischarging by non-cognate synthetases. Such identity sets were discovered in the tRNAs of a few model organisms, and their properties were generalized as universal identity rules. Since then, the panel of identity elements governing the accuracy of tRNA aminoacylation has expanded considerably, but the increasing number of reported functional idiosyncrasies has led to some confusion. In parallel, the description of other processes involving tRNAs, often well beyond aminoacylation, has progressed considerably, greatly expanding their interactome and uncovering multiple novel identities on the same tRNA molecule. This review highlights key findings on the mechanistics and evolution of tRNA and tRNA-like identities. In addition, new methods and their results for searching sets of multiple identities on a single tRNA are discussed. Taken together, this knowledge shows that a comprehensive understanding of the functional role of individual and collective nucleotide identity sets in tRNA molecules is needed for medical, biotechnological and other applications.

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Section: Expanding the World Of Trna Identitymentioning

confidence: 99%

The tRNA identity landscape for aminoacylation and beyond

Giegé

Eriani

2023

Nucleic Acids Research

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“…m 2 G can also be found at position 6 and 7 in the acceptor stem of higher eukaryotes ( 133 , 135 ). The single methyl group on N 2 of G 10 does not interfere with the triple base pairing between G 10 -C 25 -G 45 , but the hydrophobic character of the methyl group might stabilize the D-loop ( 132 , 136 ). Dimethylation of G 26 prevents base pairing with cytidine but still allows pairing with any other nucleotide ( 132 , 137 ).…”

Section: Rna Modifications and Their Influence On The Folding/stabili...mentioning

confidence: 99%

The diverse structural modes of tRNA binding and recognition

Biela

Hammermeister

Kaczmarczyk

et al. 2023

Journal of Biological Chemistry

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N 2-methylguanosine modifications on human tRNAs and snRNA U6 are important for cell proliferation, protein translation and pre-mRNA splicing

Wang

Herzel

Pythoud

et al. 2023

Nucleic Acids Research

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Modified nucleotides in non-coding RNAs, such as tRNAs and snRNAs, represent an important layer of gene expression regulation through their ability to fine-tune mRNA maturation and translation. Dysregulation of such modifications and the enzymes installing them have been linked to various human pathologies including neurodevelopmental disorders and cancers. Several methyltransferases (MTases) are regulated allosterically by human TRMT112 (Trm112 in Saccharomyces cerevisiae), but the interactome of this regulator and targets of its interacting MTases remain incompletely characterized. Here, we have investigated the interaction network of human TRMT112 in intact cells and identify three poorly characterized putative MTases (TRMT11, THUMPD3 and THUMPD2) as direct partners. We demonstrate that these three proteins are active N2-methylguanosine (m2G) MTases and that TRMT11 and THUMPD3 methylate positions 10 and 6 of tRNAs, respectively. For THUMPD2, we discovered that it directly associates with the U6 snRNA, a core component of the catalytic spliceosome, and is required for the formation of m2G, the last ‘orphan’ modification in U6 snRNA. Furthermore, our data reveal the combined importance of TRMT11 and THUMPD3 for optimal protein synthesis and cell proliferation as well as a role for THUMPD2 in fine-tuning pre-mRNA splicing.

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Required Elements in tRNA for Methylation by the Eukaryotic tRNA (Guanine-N2-) Methyltransferase (Trm11-Trm112 Complex)

Cited by 6 publications

References 82 publications

The tRNA identity landscape for aminoacylation and beyond

The tRNA identity landscape for aminoacylation and beyond

The diverse structural modes of tRNA binding and recognition

N 2-methylguanosine modifications on human tRNAs and snRNA U6 are important for cell proliferation, protein translation and pre-mRNA splicing

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