{"id":14683,"date":"2018-11-02T10:34:08","date_gmt":"2018-11-02T09:34:08","guid":{"rendered":"https:\/\/news.embl.de\/?p=14683"},"modified":"2024-03-22T11:24:57","modified_gmt":"2024-03-22T10:24:57","slug":"eric","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/eric\/","title":{"rendered":"Catching up on protein dynamics"},"content":{"rendered":"\n<p>RNA-binding proteins (RBPs) play essential roles in a variety of cellular functions including gene expression. Identifying and understanding the functions and regulation of RBPs is therefore key to unravelling the physiology of cells and determining what can go wrong in disease. A method called RNA-interactome capture (RIC), developed in the <a href=\"https:\/\/www.embl.de\/research\/units\/directors_research\/hentze\/\">Hentze group<\/a> at EMBL, has in recent years fundamentally changed our understanding of RBPs. The RIC technique involves shining ultraviolet light on living cells, which creates cross-linkages between RNA and proteins that are in direct contact with each other. Proteins attached to polyadenylated RNAs are then captured using an oligo(dT) probe against the poly(A) tails of RNAs and identified by mass spectrometry. RIC led to the discovery of hundreds of new RBPs, among them metabolic enzymes that were not previously known to bind RNA.<\/p>\n\n\n\n<p>Now, Joel Perez-Perri and colleagues in the Hentze group have enhanced the existing method. The scientists have modified the capture probe by replacing dT with locked nucleic acids \u2013 a modified type of RNA \u2013 which offer an increased affinity for target RNA, allowing for more stringent purification conditions. The technique was also adapted to reduce material requirements.<\/p>\n\n\n\n<p>Called enhanced RNA-interactome capture (eRIC), this new method boosts the identification of RBPs and, most importantly, allows the characterisation of dynamic responses of RBPs that would escape classic RIC experiments. The scientists plan to use this technique to characterise RBP dynamics in biological and pharmacological applications. For example, eRIC is being applied to human and mouse primary samples to unravel novel mechanisms involved in tumorigenesis and T cell function. eRIC has also been patented for use in other academic and commercial settings.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>The Hentze Lab enhanced a RNA-interactome capture technique to pave the way towards medical progress<\/p>\n","protected":false},"author":63,"featured_media":14685,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[43,406,490,616,70],"embl_taxonomy":[],"class_list":["post-14683","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-heidelberg","tag-hentze","tag-metabolism","tag-protein","tag-rna"],"acf":{"article_intro":"<p>Enhanced technique paves the way towards medical progress<\/p>\n","related_links":[{"link_description":"Hentze Group","link_url":"https:\/\/www.embl.de\/research\/units\/directors_research\/hentze\/"},{"link_description":"Discovering protein smartphones","link_url":"https:\/\/news.embl.de\/science\/1607-rbdmap\/"},{"link_description":"New way to isolate DNA- and RNA-protein complexes","link_url":"https:\/\/news.embl.de\/science\/new-method-isolate-dna-rna-protein-complexes\/"}],"article_sources":[{"source_description":"<p>Joel I. Perez-Perri et al.,\u00a0Discovery of RNA-binding proteins and characterization of their dynamic responses by enhanced RNA interactome capture, published online 23 October 2018, Doi: 10.1038\/s41467-018-06557-8<\/p>\n<h1 class=\"tighten-line-height small-space-below\" data-test=\"article-title\" data-article-title=\"\"><\/h1>\n","source_link_url":"https:\/\/doi.org\/10.1038\/s41467-018-06557-8"}],"vf_locked":false,"featured":false,"color":"#007B53"},"embl_taxonomy_terms":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.2 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>Catching up on protein dynamics | EMBL<\/title>\n<meta name=\"description\" content=\"The Hentze Lab enhanced an existing RNA-interactome capture technique to pave the way towards medical progress.\" \/>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.embl.org\/news\/science\/eric\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Catching up on protein dynamics | EMBL\" \/>\n<meta property=\"og:description\" content=\"The Hentze Lab enhanced an existing RNA-interactome capture technique to pave the way towards medical progress.\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.embl.org\/news\/science\/eric\/\" \/>\n<meta property=\"og:site_name\" content=\"EMBL\" \/>\n<meta property=\"article:publisher\" content=\"https:\/\/www.facebook.com\/embl.org\/\" \/>\n<meta property=\"article:published_time\" content=\"2018-11-02T09:34:08+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2024-03-22T10:24:57+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2018\/11\/Protein_ADAR_PDB_1qbj.png\" \/>\n\t<meta property=\"og:image:width\" content=\"620\" \/>\n\t<meta property=\"og:image:height\" content=\"483\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/png\" \/>\n<meta name=\"author\" content=\"Patrick Mueller\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:creator\" content=\"@embl\" \/>\n<meta name=\"twitter:site\" content=\"@embl\" \/>\n<meta name=\"twitter:label1\" content=\"Written by\" \/>\n\t<meta name=\"twitter:data1\" content=\"Patrick Mueller\" \/>\n\t<meta name=\"twitter:label2\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data2\" content=\"1 minute\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\/\/schema.org\",\"@graph\":[{\"@type\":\"NewsArticle\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/eric\/#article\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/eric\/\"},\"author\":{\"name\":\"Patrick Mueller\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/20e24fdaf3fdbf34c02236ad1afe73f2\"},\"headline\":\"Catching up on protein dynamics\",\"datePublished\":\"2018-11-02T09:34:08+00:00\",\"dateModified\":\"2024-03-22T10:24:57+00:00\",\"mainEntityOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/eric\/\"},\"wordCount\":279,\"publisher\":{\"@id\":\"https:\/\/www.embl.org\/news\/#organization\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/eric\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2018\/11\/Protein_ADAR_PDB_1qbj.png\",\"keywords\":[\"heidelberg\",\"hentze\",\"metabolism\",\"protein\",\"rna\"],\"articleSection\":[\"Science\",\"Science &amp; 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