{"id":7325,"date":"2016-07-28T11:25:31","date_gmt":"2016-07-28T09:25:31","guid":{"rendered":"http:\/\/news.embl.de\/?p=7325"},"modified":"2024-03-25T10:18:08","modified_gmt":"2024-03-25T09:18:08","slug":"1607-rbdmap","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/1607-rbdmap\/","title":{"rendered":"Discovering protein smartphones"},"content":{"rendered":"\n<p>Some proteins are less like landlines and more like smartphones: they can do more than just talk to other proteins. One molecular app of particular interest is the &#8216;RNA-binding domain&#8217;, which lets proteins engage with RNA and influence how a cell responds to its environment. Lots of proteins use it \u2013 even ones that do not appear to have one. So how do you find an app that is clearly in use but has an invisible launch site? Researchers at EMBL invented a technique to do just that. Called RBDmap, the new method was recently published in <em>Molecular Cell<\/em>.<\/p>\n\n\n\n<p>\u201cWe are one step closer to understanding how RNA and proteins interact,\u201d says Matthias Hentze, who led the study.<\/p>\n\n\n\n<p>Decades of research in the RNA field confirmed that proteins of a certain architecture can bind to RNA. But when the Hentze lab systematically searched for proteins that are able to bind to RNA using next generation methods, they saw something surprising: many of the proteins they discovered did not have any signature that could explain their RNA-binding ability. And yet, these enigmRBPs \u2013 as they came to be called \u2013 could still bind to RNA. But how? And why?<\/p>\n\n\n\n<blockquote class=\"vf-blockquote\"><p>We are one step closer to understanding how RNA and proteins interact<\/p><\/blockquote>\n\n\n\n<p>In order to answer these questions, the EMBL scientists first needed to figure out which part of these enigmatic proteins does the binding in the first place. That\u2019s where RBDmap comes in.<\/p>\n\n\n\n<p>Think of RNA-binding proteins as people holding onto a single rope \u2013 a strand of RNA. The hands holding the rope represent the part of the protein that can interact with RNA, while the rest of the body is free to do something else. \u201cRBDmap separates the hands from the rest of the body and identifies what these hands are and to whom they belong,\u201d explains Alfredo Castello, who developed the technique as a staff scientist in <a href=\"http:\/\/www.embl.de\/research\/units\/directors_research\/hentze\/index.html\">Hentze\u2019s lab<\/a>. \u201cIt tells us exactly what part of the protein binds to RNA.\u201d<\/p>\n\n\n\n<p>Using this new approach, Hentze, Castello and colleagues mapped over one thousand previously unrecognised RNA-binding sites within 529 proteins. With this information, the researchers look forward to investigating how these RNA-binding proteins work. \u201cIf we can change a very small part of the protein, chances are it can no longer bind to RNA,\u201d Hentze said. \u201cBut, the protein can still do its other jobs \u2013 which may be vital for the cell\u2019s survival,\u201d Hentze said. From these mutations, the researchers can begin to investigate the role of RNA binding in how cells respond to physiological stresses such as starvation and disease.<\/p>\n\n\n<hr class=\"vf-divider\"\/>\n\n\n<p>Castello is presently leading his own lab at the University of Oxford.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>New technique reveals uncharted docking sites in RNA-binding proteins<\/p>\n","protected":false},"author":39,"featured_media":7327,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[50,43,406,70],"embl_taxonomy":[],"class_list":["post-7325","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-biochemistry","tag-heidelberg","tag-hentze","tag-rna"],"acf":{"article_intro":"<p>New technique invented by EMBL researchers reveals uncharted docking sites in RNA-binding proteins<\/p>\n","related_links":[{"link_description":"Hentze group, EMBL ","link_url":"http:\/\/www.embl.de\/research\/units\/directors_research\/hentze\/index.html"},{"link_description":"Castello research group, University of Oxford","link_url":"http:\/\/www.bioch.ox.ac.uk\/aspsite\/index.asp?pageid=1141"}],"article_sources":[{"source_description":"<p>Castello A,\u00a0Fischer B,\u00a0<em>et al. Molecular Cell<\/em>, 21 July 2016.\u00a0DOI:10.1016\/j.molcel.2016.06.029<\/p>\n","source_link_url":"http:\/\/www.cell.com\/molecular-cell\/fulltext\/S1097-2765(16)30287-8"}],"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>Discovering protein smartphones with RBDmap<\/title>\n<meta name=\"description\" content=\"A new technique, RBDmap, invented by researchers in the Hentze group at EMBL reveals uncharted docking sites in RNA-binding proteins\" \/>\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\/1607-rbdmap\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Discovering protein smartphones with RBDmap\" \/>\n<meta property=\"og:description\" content=\"A new technique, RBDmap, invented by researchers in the Hentze group at EMBL reveals uncharted docking sites in RNA-binding proteins\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.embl.org\/news\/science\/1607-rbdmap\/\" \/>\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=\"2016-07-28T09:25:31+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2024-03-25T09:18:08+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2016\/07\/1607-hentze-ib.jpg\" \/>\n\t<meta property=\"og:image:width\" content=\"620\" \/>\n\t<meta property=\"og:image:height\" content=\"425\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/jpeg\" \/>\n<meta name=\"author\" content=\"Margaux Phares\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:creator\" content=\"@mxphares\" \/>\n<meta name=\"twitter:site\" content=\"@embl\" \/>\n<meta name=\"twitter:label1\" content=\"Written by\" \/>\n\t<meta name=\"twitter:data1\" content=\"Margaux Phares\" \/>\n\t<meta name=\"twitter:label2\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data2\" content=\"2 minutes\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\/\/schema.org\",\"@graph\":[{\"@type\":\"NewsArticle\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/1607-rbdmap\/#article\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/1607-rbdmap\/\"},\"author\":{\"name\":\"Margaux Phares\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/d1fced3e1bf469536cf90385bd640f83\"},\"headline\":\"Discovering protein smartphones\",\"datePublished\":\"2016-07-28T09:25:31+00:00\",\"dateModified\":\"2024-03-25T09:18:08+00:00\",\"mainEntityOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/1607-rbdmap\/\"},\"wordCount\":446,\"publisher\":{\"@id\":\"https:\/\/www.embl.org\/news\/#organization\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/1607-rbdmap\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2016\/07\/1607-hentze-ib.jpg\",\"keywords\":[\"biochemistry\",\"heidelberg\",\"hentze\",\"rna\"],\"articleSection\":[\"Science\",\"Science &amp; 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