The methyltransferase TrmA facilitates tRNA folding through interaction with its RNA-binding domain

Autor: Emily F Soon, Laura Carole Keffer-Wilkes, Ute Kothe

Publikováno v: Nucleic Acids Research

tRNAs are the most highly modified RNAs in all cells, and formation of 5-methyluridine (m5U) at position 54 in the T arm is a common RNA modification found in all tRNAs. The m5U modification is generated by the methyltransferase TrmA. Here, we test a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32cc5377e3386a63fcd24015d884087a
https://doi.org/10.1093/nar/gkaa548

New tRNA contacts facilitate ligand binding in a Mycobacterium smegmatis T box riboswitch

Autor: Frank J. Grundy, Jane K. Frandsen, Tina M. Henkin, Anna V. Sherwood

Publikováno v: Proceedings of the National Academy of Sciences. 115:3894-3899

T box riboswitches are RNA regulatory elements widely used by organisms in the phyla Firmicutes and Actinobacteria to regulate expression of amino acid-related genes. Expression of T box family genes is down-regulated by transcription attenuation or

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d7c8cb4f0b45c1e202e8f9cacfbf4fd6
https://doi.org/10.1073/pnas.1721254115

Unique localization of the plastid-specific ribosomal proteins in the chloroplast ribosome small subunit provides mechanistic insights into the chloroplastic translation

Autor: Jian Shi, Shashi Bhushan, Tofayel Ahmed

Publikováno v: Nucleic Acids Research

Chloroplastic translation is mediated by a bacterial-type 70S chloroplast ribosome. During the evolution, chloroplast ribosomes have acquired five plastid-specific ribosomal proteins or PSRPs (cS22, cS23, bTHXc, cL37 and cL38) which have been suggest

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7229e07a0de8cd7df93087192c6cacf7
https://doi.org/10.1093/nar/gkx499

Duplication of Drosophila melanogaster mitochondrial EF-Tu: pre-adaptation to T-arm truncation and exclusion of bulky aminoacyl residues

Autor: Takuma Suematsu, Yoh-ichi Watanabe, Kimitsuna Watanabe, Takashi Ohtsuki, Tsutomu Suzuki, Koh Ki Aihara, Aya Sato, Kiyoshi Kita

Publikováno v: Biochemical Journal. 474:957-969

Translation elongation factor Tu (EF-Tu) delivers aminoacyl-tRNA to ribosomes in protein synthesis. EF-Tu generally recognizes aminoacyl moieties and acceptor- and T-stems of aminoacyl-tRNAs. However, nematode mitochondrial (mt) tRNAs frequently lack

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5893dd25ed1967f2d1d0c3f0ee8fa284
https://doi.org/10.1042/bcj20160929

Methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response inPseudomonas aeruginosa

Autor: Narumon Thongdee, Julien Lescar, Juthamas Jaroensuk, Michael S. DeMott, Chong Wai Liew, Mayuree Fuangthong, Yee Hwa Wong, Yok Hian Chionh, Sopapan Atichartpongkul, Skorn Mongkolsuk, Peter C. Dedon, Megan E. McBee, Erin G. Prestwich

Publikováno v: Nucleic Acids Research
Nucleic Acids Research, 2016, 44 (22), pp.10834-10848. ⟨10.1093/nar/gkw870⟩
Oxford University Press
Nucleic Acids Research, Oxford University Press, 2016, 44 (22), pp.10834-10848. ⟨10.1093/nar/gkw870⟩

Bacteria respond to environmental stresses using a variety of signaling and gene expression pathways, with translational mechanisms being the least well understood. Here, we identified a tRNA methyltransferase in Pseudomonas aeruginosa PA14, trmJ, wh

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3ca8694e4caaaaf4dfd2356adbe83a5
https://doi.org/10.1093/nar/gkw870