Open AccessJournal Article
Recent progress of structural biology of tRNA processing and modification.
Kotaro Nakanishi,Osamu Nureki +1 more
TLDR
The recent progress of the structural biology of the tRNA processing and modification is reviewed and it is proposed that modification procedure itself contributes to the RNA (re)folding, where the modification enzymes function as a kind of RNA chaperones.Abstract:
Transfer RNA (tRNA) is a key molecule to decode the genetic information on mRNA to amino aicds (protein), in a ribosome. For tRNA to fulfill its adopter function, tRNA should be processed into the standard length, and be post-transcriptionally modified. This modification step is essential for the tRNA to maintain the canonical L-shaped structure, which is required for the decoding function of tRNA. Otherwise, it has recently been proposed that modification procedure itself contributes to the RNA (re)folding, where the modification enzymes function as a kind of RNA chaperones. Recent genome analyses and post-genome (proteomics and transcriptomics) analyses have identified genes involved in the tRNA processings and modifications. Furthermore, post-genomic structural analysis has elucidated the structural basis for the tRNA maturation mechanism. In this paper, the recent progress of the structural biology of the tRNA processing and modification is reviewed.read more
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References
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Journal ArticleDOI
Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme.
TL;DR: Structural comparisons with TruB demonstrate that all Psi synthases are descended from a common molecular ancestor.
Journal ArticleDOI
Crystal structure of the specificity domain of Ribonuclease P
TL;DR: The structure of the 154-nucleotide specificity domain of Bacillus subtilis RNase P is reported, revealing the architecture of this domain, the interactions that maintain the overall fold of the molecule, a large non-helical but well-structured module that is conserved in allRNase P RNA, and the regions that are involved in interactions with the substrate.
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Alternative Tertiary Structure of tRNA for Recognition by a Posttranscriptional Modification Enzyme
Ryuichiro Ishitani,Osamu Nureki,Nobukazu Nameki,Norihiro Okada,Susumu Nishimura,Shigeyuki Yokoyama +5 more
TL;DR: The crystal structure of tRNA bound with archaeosine tRNA-guanine transglycosylase is determined, which modifies G15 of the D arm in the core of the core, by counting the nucleotide number from G1 to G15 in the lambda form.
Journal ArticleDOI
Basis for structural diversity in homologous RNAs.
TL;DR: A crystal structure of the 161-nucleotide specificitydomain of an A-type ribonuclease P that differs in secondary and tertiary structure from the specificity domain of a B-type molecule is reported.
Journal ArticleDOI
Structural basis for substrate binding, cleavage and allostery in the tRNA maturase RNase Z
TL;DR: The crystal structure of Bacillus subtilis RNase Z is reported, and a mechanism for tRNA recognition and cleavage is proposed, which highlights the extraordinary adaptability of the metallo-hydrolase domain of the β-lactamase family for the hydrolysis of covalent bonds.