Abstract
To date, numerous modified nucleosides in tRNA as well as tRNA modification enzymes have been identified not only in thermophiles but also in mesophiles. Because most modified nucleosides in tRNA from thermophiles are common to those in tRNA from mesophiles, they are considered to work essentially in steps of protein synthesis at high temperatures. At high temperatures, the structure of unmodified tRNA will be disrupted. Therefore, thermophiles must possess strategies to stabilize tRNA structures. To this end, several thermophile-specific modified nucleosides in tRNA have been identified. Other factors such as RNA-binding proteins and polyamines contribute to the stability of tRNA at high temperatures. Thermus thermophilus, which is an extreme-thermophilic eubacterium, can adapt its protein synthesis system in response to temperature changes via the network of modified nucleosides in tRNA and tRNA modification enzymes. Notably, tRNA modification enzymes from thermophiles are very stable. Therefore, they have been utilized for biochemical and structural studies. In the future, thermostable tRNA modification enzymes may be useful as biotechnology tools and may be utilized for medical science.
Highlights
Transfer RNA is an adaptor molecule required for the conversion of genetic information encoded by nucleic acids into amino acid sequences of proteins [1,2]
We focus on the modified nucleosides and tRNA modification enzymes from thermophiles including the difficulties in sequencing the rigid and stable tRNAs from thermophiles
Since the tRNA modifications in moderate thermophiles are essentially similar to those in mesophiles, we describe them separately from extreme-thermophiles and hyper-thermophiles
Summary
Transfer RNA is an adaptor molecule required for the conversion of genetic information encoded by nucleic acids into amino acid sequences of proteins [1,2]. UV resistance Stabilization of D-arm structure (see main text) Sulfur-containing modifications in tRNA are reviewed in Reference [35]. Stabilization of three-dimensional core structure The presence of m22Gm has been confirmed in nucleosides of a tRNA mixture from several thermophilic archaea [56,97,98,99,100]. Alteration of codon–anticodon interaction (Arhaeoglobus fulgidus and Haloarcula marismourtui) Change of recognition by aminoacyl-tRNA synthetase (Arhaeoglobus fulgidus and Haloarcula marismourtui) Decoding of AUA codons by k2C34 and agm2C34 modifications is reviewed in References [114,115]. Prevention of frame-shift error Reinforcement of codon–anticodon interaction Recognition by aminoacyl-tRNA synthetases i6A derivatives are reviewed in Reference [197]. Stabilization of three-dimensional core In the case of T. thermophilus, m7G46 modification functions a key factor in a network between modified nucleosides in tRNA and tRNA modification enzymes (see main text) [11]
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