Modification of the wobble uridine in bacterial and mitochondrial tRNAs reading NNA/NNG triplets of 2-codon boxes

Armengod, M.-Eugenia; Meseguer, Salvador; Villarroya, Magda; Díaz‐Prado, Silvia; Moukadiri, Ismaïl; Ruiz-Partida, Rafael; Garzón, María José; Navarro-González, Carmen; Martínez-Zamora, Ana

doi:10.4161/15476286.2014.992269

Cited by 63 publications

(117 citation statements)

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“…Further studies also suggest that nucleotide-induced changes in conformation and oligomerization of the GidA/MnmE complex are an integral part of the tRNA modification reaction cycle [41]. Much work is needed, however, to elucidate the exact molecular mechanism of the GidA/MnmE interaction and subsequent tRNA modification [15,42].…”

Section: Rna Modifications By Enzymes Encoded By the Gid Operonmentioning

confidence: 94%

RNA modification enzymes encoded by the gid operon: Implications in biology and virulence of bacteria

Shippy

Fadl

2015

Microbial Pathogenesis

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Section: Rna Modifications By Enzymes Encoded By the Gid Operonmentioning

confidence: 94%

RNA modification enzymes encoded by the gid operon: Implications in biology and virulence of bacteria

Shippy

Fadl

2015

Microbial Pathogenesis

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“…The xm 5 U modification at the wobble position of an anticodon in tRNA is complex and is synthesized by multiple steps [67,68]. In the case of E. coli , a portion of cmnm 5 U34 in tRNA Leu cnmn 5 UAA and C34 in tRNA Leu CAA is modified to cmnm 5 Um34 and Cm34, respectively, by TrmL [14].…”

Section: Transfer Rna Recognition Mechanismmentioning

confidence: 99%

Transfer RNA methyltransferases with a SpoU‐TrmD (SPOUT) fold and their modified nucleosides in tRNA

Hori

2017

Biomolecules

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The existence of SpoU-TrmD (SPOUT) RNA methyltransferase superfamily was first predicted by bioinformatics. SpoU is the previous name of TrmH, which catalyzes the 2’-O-methylation of ribose of G18 in tRNA; TrmD catalyzes the formation of N1-methylguanosine at position 37 in tRNA. Although SpoU (TrmH) and TrmD were originally considered to be unrelated, the bioinformatics study suggested that they might share a common evolution origin and form a single superfamily. The common feature of SPOUT RNA methyltransferases is the formation of a deep trefoil knot in the catalytic domain. In the past decade, the SPOUT RNA methyltransferase superfamily has grown; furthermore, knowledge concerning the functions of their modified nucleosides in tRNA has also increased. Some enzymes are potential targets in the design of anti-bacterial drugs. In humans, defects in some genes may be related to carcinogenesis. In this review, recent findings on the tRNA methyltransferases with a SPOUT fold and their methylated nucleosides in tRNA, including classification of tRNA methyltransferases with a SPOUT fold; knot structures, domain arrangements, subunit structures and reaction mechanisms; tRNA recognition mechanisms, and functions of modified nucleosides synthesized by this superfamily, are summarized. Lastly, the future perspective for studies on tRNA modification enzymes are considered.

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“…In particular, modified nucleosides of the anticodon loop transform the loop architecture and dynamics to meet the requirements that the ribosome places on all tRNAs [2,4,5]. In Escherichia coli , the MnmEG complex, formed by the dimeric proteins MnmE and MnmG [6], modifies the wobble uridine (U34) of tRNA Lys UUU , tRNA Glu UUC , tRNA Gln UUG , tRNA Leu UAA , tRNA Arg UCU , and tRNA Gly UCC [7,8]. MnmEG catalyzes the incorporation of either an aminomethyl (nm) or a carboxymethylaminomethyl (cmnm) group at position 5 of U34 using ammonium or glycine as substrate (Figure 1) [7].…”

Section: Introductionmentioning

confidence: 99%

Bacillus subtilis exhibits MnmC-like tRNA modification activities

et al. 2018

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The MnmE-MnmG complex of Escherichia coli uses either ammonium or glycine as a substrate to incorporate the 5-aminomethyl or 5-carboxymethylaminomethyl group into the wobble uridine of certain tRNAs. Both modifications can be converted into a 5-methylaminomethyl group by the independent oxidoreductase and methyltransferase activities of MnmC, which respectively reside in the MnmC(o) and MnmC(m) domains of this bifunctional enzyme. MnmE and MnmG, but not MnmC, are evolutionarily conserved. Bacillus subtilis lacks genes encoding MnmC(o) and/or MnmC(m) homologs. The glycine pathway has been considered predominant in this typical gram-positive species because only the 5-carboxymethylaminomethyl group has been detected in tRNALysUUU and bulk tRNA to date. Here, we show that the 5-methylaminomethyl modification is prevalent in B. subtilis tRNAGlnUUG and tRNAGluUUC. Our data indicate that B. subtilis has evolved MnmC(o)- and MnmC(m)-like activities that reside in non MnmC homologous protein(s), which suggests that both activities provide some sort of biological advantage.

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Modification of the wobble uridine in bacterial and mitochondrial tRNAs reading NNA/NNG triplets of 2-codon boxes

Abstract: (2014) Modification of the wobble uridine in bacterial and mitochondrial tRNAs reading NNA/NNG triplets of 2-codon boxes, RNA Biology, 11:12, 1495-1507

Cited by 63 publications

References 113 publications

RNA modification enzymes encoded by the gid operon: Implications in biology and virulence of bacteria

RNA modification enzymes encoded by the gid operon: Implications in biology and virulence of bacteria

Transfer RNA methyltransferases with a SpoU‐TrmD (SPOUT) fold and their modified nucleosides in tRNA

Bacillus subtilis exhibits MnmC-like tRNA modification activities

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