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The crystal structure of Pyrococcus abyssi tRNA (uracil-54, C5)-methyltransferase provides insights into its tRNA specificity.
Walbott H, Leulliot N, Grosjean H, Golinelli-Pimpaneau B. Walbott H, et al. Nucleic Acids Res. 2008 Sep;36(15):4929-40. doi: 10.1093/nar/gkn437. Epub 2008 Jul 24. Nucleic Acids Res. 2008. PMID: 18653523 Free PMC article.
A positively charged groove at the interface between the three domains probably locates part of the tRNA-binding site of (Pab)TrmU54. We show that a mini-tRNA lacking both the D and anticodon stem-loops is recognized by (Pab)TrmU54. These results were used to model …
A positively charged groove at the interface between the three domains probably locates part of the tRNA-binding site of (Pab)TrmU54. …
Decoding Substrate Selectivity of an Archaeal RlmCD-like Methyltransferase Through Its Salient Traits.
Saha S, Kanaujia SP. Saha S, et al. Biochemistry. 2024 Oct 1;63(19):2477-2492. doi: 10.1021/acs.biochem.4c00401. Epub 2024 Sep 18. Biochemistry. 2024. PMID: 39350642
Among these, a tRNA-specific Arm(5)U MTase ((Pab)TrmU54) has already been characterized. This study focused on the structural and functional characterization of the rRNA-specific Arm(5)U MTase from the hyperthermophilic archaeon Pyrococcus horikoshii (PhRlmCD). ...
Among these, a tRNA-specific Arm(5)U MTase ((Pab)TrmU54) has already been characterized. This study focused on the structural and fun …
Acquisition of a bacterial RumA-type tRNA(uracil-54, C5)-methyltransferase by Archaea through an ancient horizontal gene transfer.
Urbonavicius J, Auxilien S, Walbott H, Trachana K, Golinelli-Pimpaneau B, Brochier-Armanet C, Grosjean H. Urbonavicius J, et al. Mol Microbiol. 2008 Jan;67(2):323-35. doi: 10.1111/j.1365-2958.2007.06047.x. Epub 2007 Dec 7. Mol Microbiol. 2008. PMID: 18069966 Free article.
None of the gene products of the two P. abyssi paralogues catalyses in vitro the formation of m(5)U in a P. abyssi rRNA fragment homologous to the bacterial RumA substrate. Instead, PAB0719 enzyme (renamed (Pab)TrmU54) displays an identical specificity to TrmA, as it catal …
None of the gene products of the two P. abyssi paralogues catalyses in vitro the formation of m(5)U in a P. abyssi rRNA fragment homologous …