{"id":16592,"date":"2019-07-11T08:32:20","date_gmt":"2019-07-11T06:32:20","guid":{"rendered":"https:\/\/news.embl.de\/?p=16592"},"modified":"2024-03-22T10:56:28","modified_gmt":"2024-03-22T09:56:28","slug":"a-trna-modifier-at-work","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/a-trna-modifier-at-work\/","title":{"rendered":"A tRNA modifier at work"},"content":{"rendered":"\n

All living cells employ ribosomes and transfer RNA (tRNA) molecules to decode messenger RNA (mRNA) sequences and translate the genetic information into correctly assembled and functional proteins. It\u2019s crucial for cells to produce these proteins at the right speed to avoid protein misfolding and aggregation within cells, which has been linked to a number of neurodegenerative diseases and cancer. The modification of tRNA molecules by specialised enzymes is one way to regulate the production speed to the correct pace.<\/p>\n\n\n\n

Elongator: a large protein complex<\/h2>\n\n\n\n

Scientists from the M\u00fcller group <\/a>at EMBL Heidelberg and the Kosinski group<\/a> at EMBL Hamburg, in collaboration with researchers at the Ma\u0142opolska Centre of Biotechnology<\/a> (MCB) at the Jagiellonian University<\/a> in Krak\u00f3w, Poland, and at Martin Luther University Halle-Wittenberg<\/a>, Germany, have now managed to catch a crucial component of the tRNA modification machinery directly at work. Using cryo-electron microscopy (cryo-EM), they have determined the structure of a large protein complex called Elongator, in the presence and absence of its natural substrate tRNA.<\/p>\n\n\n\n

Their results, published in Science Advances<\/em><\/a>, are valuable for the protein synthesis research community. They allow for a more complete understanding of one of the key mechanisms in ribosome-mediated protein synthesis, where tRNA plays a central role as an adaptor molecule \u2013 it forms the physical link between mRNA and the amino acids to be assembled into proteins.<\/p>\n\n\n\n

\"Elongator
Cryo-EM structure of Elp123 bound to tRNA with co-factors SAM and acetyl-COA participating in the modification of U34 tRNA. IMAGE: Marcin Jaciuk\/MCB<\/figcaption><\/figure><\/div>\n\n\n\n

Medical implications<\/h2>\n\n\n\n

\u201cAfter 10 years of research on this large cellular machine, we finally start to have a clearer picture of the complicated interplay between the different Elongator subunits and the bound substrate tRNA, which permits the modification reaction,\u201d says group leader Christoph M\u00fcller.<\/p>\n\n\n\n

Mutations in any of the six subunits of Elongator are associated with the onset of human diseases, including familial dysautonomia (a disease of the nervous system), obesity, bronchial asthma, intellectual disability, ventricular hypertrophy, Rolandic epilepsy and cancer. Thus, its potential as a drug target is ripe for exploration. \u201cOur structural work tells us how the tRNA is specifically positioned in the active site of the complex, but also allows a structure-based design of specific drug molecules that might cure Elongator-related diseases in the future,\u201d says co-author Sebastian Glatt, a former postdoc in the M\u00fcller group, who now leads the Max Planck Research Group at MCB. Glatt is currently involved in setting up the first cryo-EM facility in Poland \u2013 an EMBL member state since February this year<\/a>.<\/p>\n\n\n\n

Integrative modelling<\/h2>\n\n\n\n

For the Kosinski group, the cryo-EM structure of Elongator marks another success. Two years ago, they published a model of Elongator built using a computational modelling method developed by Jan Kosinski. Comparing this model with the high-resolution cryo-EM structure shows a remarkable similarity between them \u2013 a clear demonstration of the power of so-called integrative modelling methods, which model structures based on data from various experiments. \u201cWe are very excited by the accuracy of the model, and are now working towards publishing our methods as easy-to-use software,\u201d says Jan Kosinski. The group is also organising an EMBO Practical Course<\/a>, to take place in November, where such integrative methods will be taught.<\/p>\n\n\n

\n

Register for the EMBO Practical course, \u2018Practical integrative structural biology\u2019<\/a>, 3\u20139 November 2019<\/p>\n

Register for the EMBL Course, \u2018Cryo-Electron Microscopy and 3D Image Processing\u2019<\/a>, 23\u201331 August 2020<\/p>\n

<\/p><\/div>\n","protected":false},"excerpt":{"rendered":"

Using cryo-EM, scientists have determined the structure of a large protein complex called Elongator.<\/p>\n","protected":false},"author":68,"featured_media":16580,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[718,875,53,43,876,540,441,539,35],"embl_taxonomy":[18861,9796,19341],"class_list":["post-16592","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-cryo-em","tag-elongator","tag-hamburg","tag-heidelberg","tag-integrative-modelling","tag-kosinski","tag-muller","tag-research-highlight","tag-structural-biology","embl_taxonomy-christoph-muller","embl_taxonomy-embl-heidelberg","embl_taxonomy-muller-group"],"acf":{"article_intro":"

Cryo-EM reveals the structure of a piece of cellular machinery with important medical implications<\/p>\n","related_links":[{"link_description":"Research in the Structural and Computational Biology Unit","link_url":"https:\/\/www.embl.de\/research\/units\/scb\/index.html"},{"link_description":"Research at EMBL Hamburg","link_url":"https:\/\/www.embl-hamburg.de\/research\/index.php"},{"link_description":"EMBL's Cryo-Electron Microscopy Service Platform","link_url":"https:\/\/www.embl.de\/services\/cryo-em-platform\/"},{"link_description":"Poland's National Cryo-EM Centre","link_url":"https:\/\/synchrotron.uj.edu.pl\/en_GB\/cryo-em"}],"article_sources":[{"source_description":"

Dauden MI et al.<\/em>Molecular basis of tRNA recognition by the Elongator complex. Science Advances<\/em>. Published online 10 July 2019. DOI:\u00a010.1126\/sciadv.aaw2326<\/p>\n","source_link_url":"https:\/\/advances.sciencemag.org\/content\/5\/7\/eaaw2326"}],"vf_locked":false,"featured":false,"color":"#007B53","link_color":"#fff","show_featured_image":false,"in_this_article":false,"youtube_url":"","mp4_url":"","video_caption":"","press_contact":"None","translations":false},"embl_taxonomy_terms":[{"uuid":"a:2:{i:0;s:36:\"4428d1fd-441a-4d6d-a1c5-5dcf5665f213\";i:1;s:36:\"63333cc0-a357-4f7e-b1d5-43dc9e27227f\";}","parents":[],"name":["Christoph M\u00fcller"],"slug":"christoph-muller","description":"Who > Christoph M\u00fcller"},{"uuid":"a:3:{i:0;s:36:\"b14d3f13-5670-44fb-8970-e54dfd9c921a\";i:1;s:36:\"89e00fee-87f4-482e-a801-4c3548bb6a58\";i:2;s:36:\"ab46b6d4-71d8-49f8-b2f4-b326d4c8ea4e\";}","parents":[],"name":["EMBL Heidelberg"],"slug":"embl-heidelberg","description":"Where > All EMBL sites > EMBL 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