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en: Transfer RNA Synthesis and Regulation

ja: Transfer RNA Synthesis and Regulation

en: Encyclopedia of Life Sciences

ja: Encyclopedia of Life Sciences


en: [Review] Crystal Structure Analysis of β-Amylase/Saccharide Complexes Measured at Different pH and Room Temperature.

ja: 非凍結結晶を用いたβ-アミラーゼと基質アナログ複合体構造のpH変化の解析

en: Bulletin of Applied Glycoscience

ja: 応用糖質科学


en: X-Ray Structure of the tRNA Methyltransferase Complex of Trm7 and Trm734 from Saccharomyces cerevisiae

en: Photon Factory Highlights 2019

ja: Photon Factory Highlights 2019


en: Recent Insights Into the Structure, Function, and Evolution of the RNA-Splicing Endonucleases.

en: RNA-splicing endonuclease (EndA) cleaves out introns from archaeal and eukaryotic precursor (pre)-tRNA and is essential for tRNA maturation. In archaeal EndA, the molecular mechanisms underlying complex assembly, substrate recognition, and catalysis have been well understood. Recently, certain studies have reported novel findings including the identification of new subunit types in archaeal EndA structures, providing insights into the mechanism underlying broad substrate specificity. Further, metagenomics analyses have enabled the acquisition of numerous DNA sequences of EndAs and intron-containing pre-tRNAs from various species, providing information regarding the co-evolution of substrate specificity of archaeal EndAs and tRNA genetic diversity, and the evolutionary pathway of archaeal and eukaryotic EndAs. Although the complex structure of the heterothermic form of eukaryotic EndAs is unknown, previous reports regarding their functions indicated that mutations in human EndA cause neurological disorders including pontocerebellar hypoplasia and progressive microcephaly, and yeast EndA significantly cleaves mitochondria-localized mRNA encoding cytochrome b mRNA processing 1 (Cpb1) for mRNA maturation. This mini-review summarizes the aforementioned results, discusses their implications, and offers my personal opinion regarding future directions for the analysis of the structure and function of EndAs.

en: Frontiers in Genetics

ja: Frontiers in Genetics


en: Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA.

en: 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. , 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.

en: Microorganisms

ja: Microorganisms


en: Elucidation of structural basis for the molecular machineries responsible for RNA synthesis and processing from Archaea

ja: アーキアのRNA合成・編集加工を担う分子装置の構造基盤の解明

en: 極限環境生物学会誌 = Journal of Japanese Society for Extremophiles


en: Transfer RNA Synthesis and Regulation.'' Encyclopedia in Life Science

en: Wiley Inter-express

ja: Wiley Inter-express


en: 微生物も免疫力がつく

ja: 微生物も免疫力がつく

en: Seibutsu-kogaku Kaishi

ja: 生物工学会誌


en: Archaeal RNA polymerase.

ja: Archaeal RNA polymerase.

en: The recently solved X-ray crystal structures of archaeal RNA polymerase (RNAP) allow a structural comparison of the transcription machinery among all three domains of life. Archaeal transcription is very simple and all components, including the structures of general transcription factors and RNAP, are highly conserved in eukaryotes. Therefore, it could be a new model for the dissection of the eukaryotic transcription apparatus. The archaeal RNAP structure also provides a framework for addressing the functional role that Fe-S clusters play within the transcription machinery of archaea and eukaryotes. A comparison between bacterial and archaeal open complex models reveals likely key motifs of archaeal RNAP for DNA unwinding during the open complex formation.

en: Current Opinion in Structural Biology

ja: Current Opinion in Structural Biology


en: Archaeal transcriptional machinery

ja: 古細菌の転写装置

en: Seikagaku

ja: 生化学