{"id":2996,"date":"2015-01-07T10:46:25","date_gmt":"2015-01-07T09:46:25","guid":{"rendered":"http:\/\/news.embl.de\/?p=2996"},"modified":"2024-11-29T16:55:40","modified_gmt":"2024-11-29T15:55:40","slug":"1412_hairclip-protein","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/1412_hairclip-protein\/","title":{"rendered":"&#8216;Hairclip&#8217; protein mechanism explained"},"content":{"rendered":"\n<ul class=\"wp-block-list\"><li>New study describes, for the first time, a fundamental mechanism regulating a protein\u2019s shape.<\/li><li>\u201cHairclip\u201d mechanism involves mutations acting on one side of a protein to open or close the configuration of amino acids on the other.<\/li><li>Findings have implications for the manipulation of proteins, with potential applications in biotechnology and drug development.<\/li><\/ul>\n\n\n<hr class=\"vf-divider\"\/>\n\n\n<p>The shape of a protein determines its function, for example whether it is able to interact with another protein or with a drug. But a protein\u2019s shape is not constant \u2013 it may change in response to different conditions, or simply as a matter of course. Understanding how this process works is key to figuring out how to manipulate proteins, for example in order to disrupt a disease. This&nbsp;finding provides important clues that will help focus future research.<\/p>\n\n\n\n<p>The team looked at a family of bacterial RNA-binding proteins that control a basic process in metabolism: one type of bacteria lives in very high temperatures, and the other likes things colder. The goal was to determine how a protein morphs from an active configuration (one that lets it bind to RNA) to an inactive one in two very different environments.<\/p>\n\n\n\n<p>\u201cThe process is controlled by mutations, but these mutations aren\u2019t in an obvious place, where the binding happens,\u201d explains <a title=\"Sarah Teichmann\" href=\"http:\/\/www.ebi.ac.uk\/about\/people\/sarah-teichmann\" target=\"_blank\" rel=\"noopener noreferrer\">Sarah Teichmann, research group leader<\/a> at the European Bioinformatics Institute (EMBL-EBI) and the Wellcome Trust Sanger Institute. \u201cThey\u2019re actually working from a distance, indirectly, to change the shape of those sites. We wanted to know how that works at an atomic level.\u201d<\/p>\n\n\n\n<blockquote class=\"vf-blockquote\"><p>The process is controlled by mutations, but these mutations are not in an obvious place, where the binding happens.<\/p><\/blockquote>\n\n\n\n<p>Undertaken initially as a purely computational study, lead author Tina Perica stepped away from her laptop and into the lab, where she worked with others to fill in the picture with experiments in biophysics, and integrated structural biology to detail how these mutations work.<\/p>\n\n\n\n<p>\u201cAny stable protein will have a lot of constraints on its mutational pathways,\u201d says Perica. \u201cThese mutations have very few options \u2013 just like a person walking along a cliff will need to keep to a narrow path. But at the same time, proteins need enough wiggle room to be able to bind to things, like another protein or a drug. To find where the protein could provide that wiggle room, we retraced its steps millions of years into the past, and used a lot of different approaches to figure out what was happening.\u201d<\/p>\n\n\n\n<p>\u201cIf you know how a species of bacteria has evolved, you can reconstruct proteins that it may have had in the past, but which don\u2019t exist today,\u201d says Yasushi Kondo from MRC Laboratory of Molecular Biology. \u201cWe made a couple of these proteins, and used X-ray crystallography to solve their structures. That let us see details we would never have seen if we\u2019d only studied proteins from the bacteria that live today. When we put that new information together with computational work and simulations, we started to see a clear picture of how these proteins change.\u201d<\/p>\n\n\n\n<p>\u201cWe were really pleased to do the <a href=\"http:\/\/youtu.be\/T9LQS1G-DVc\">elastic network modelling<\/a> for this study, because it helps you see the dynamics of how the protein goes from one configuration to another,\u201d says Nathalie Reuters of the University of Bergen, Norway. \u201cIt also shows that these fluctuations are the same for natural mutations between the thermophilic and mesophilic organism, for allosteric ligands, for small molecules binding, or for engineered mutations.\u201d<\/p>\n\n\n\n<p>\u201cThese proteins provide a very good example of a fundamental biophysical phenomenon that we think can happen in many proteins, regardless of which organism,\u201d says Teichmann. \u201cWe believe our findings will help future research into manipulating proteins, which has potential applications across the life sciences.\u201d<\/p>\n\n\n\n<div class=\"vf-video\" style=\"padding-top: 0; padding-bottom: 56.25%;\">\n    <iframe loading=\"lazy\" width=\"640\" height=\"360\" src=\"https:\/\/youtube.com\/embed\/T9LQS1G-DVc\" frameborder=\"0\" allow=\"autoplay; encrypted-media\" allowfullscreen><\/iframe>\n<\/div>\n\n\n\n<p><em>This post was originally published on <a href=\"https:\/\/www.ebi.ac.uk\/about\/news\/press-releases\/hairclip-protein\" target=\"_blank\" rel=\"canonical nofollow noopener noreferrer\" data-href=\"https:\/\/www.ebi.ac.uk\/about\/news\/press-releases\/hairclip-protein\">EMBL-EBI News.<\/a><\/em><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Research led by Teichmann group identifies fundamental mechanism for controlling protein function.<\/p>\n","protected":false},"author":13,"featured_media":2998,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[65,36,32,35,51],"embl_taxonomy":[],"class_list":["post-2996","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-biophysics","tag-embl-ebi","tag-health","tag-structural-biology","tag-systems-biology"],"acf":{"article_intro":"<p>Research led by Sarah\u00a0Teichmann&#8217;s group on the Wellcome Genome Campus has identified a fundamental mechanism for controlling protein function. Published in the journal <em>Science<\/em>, the discovery has wide-ranging implications for biotechnology and medicine.<\/p>\n","related_links":[{"link_description":"Video - simulation of protein mechanism, explained by Sarah Teichmann","link_url":"https:\/\/www.youtube.com\/watch?v=T9LQS1G-DVc&feature=youtu.be"},{"link_description":"Press release on the University of Bergen website (Norwegian), 18 December 2014","link_url":"http:\/\/www.uib.no\/aktuelt\/84463\/forskere-kan-fjernstyre-proteiner"},{"link_description":"Press release on the EMBL-EBI website, 19 December 2014","link_url":"http:\/\/www.ebi.ac.uk\/about\/news\/press-releases\/hairclip-protein"},{"link_description":"Wellcome Genome Campus","link_url":"http:\/\/www.wellcome.ac.uk\/Funding\/Biomedical-science\/Funded-projects\/Major-initiatives\/Wellcome-Trust-Sanger-Institute\/Wellcome-Trust-Genome-Campus\/index.htm"}],"article_sources":[{"source_description":"<p>Perica, T., Kondo, Y, Tiwari, S.P., et al. (2014). Evolution of oligomeric state through allosteric pathways that mimic ligand binding. Science (in press). Published online 19 December 2014; doi: 10.1126\/science.1254346<\/p>\n","source_link_url":"http:\/\/europepmc.org\/abstract\/MED\/25525255"}],"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>&#039;Hairclip&#039; protein mechanism explained<\/title>\n<meta name=\"description\" content=\"Research led by Teichmann group identifies fundamental mechanism for controlling protein function.\" \/>\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\/1412_hairclip-protein\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"&#039;Hairclip&#039; protein mechanism explained\" \/>\n<meta property=\"og:description\" content=\"Research led by Teichmann group identifies fundamental mechanism for controlling protein function.\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.embl.org\/news\/science\/1412_hairclip-protein\/\" \/>\n<meta property=\"og:site_name\" content=\"EMBL\" \/>\n<meta property=\"article:publisher\" content=\"https:\/\/www.facebook.com\/embl.org\/\" \/>\n<meta property=\"article:author\" content=\"www.facebook.com\/EMBLEBI\" \/>\n<meta property=\"article:published_time\" content=\"2015-01-07T09:46:25+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2024-11-29T15:55:40+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2015\/01\/Hairclip_news_EMBL.jpg\" \/>\n\t<meta property=\"og:image:width\" content=\"620\" \/>\n\t<meta property=\"og:image:height\" content=\"465\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/jpeg\" \/>\n<meta name=\"author\" content=\"Mary Todd Bergman\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:creator\" content=\"@EMBLEBI\" \/>\n<meta name=\"twitter:site\" content=\"@embl\" \/>\n<meta name=\"twitter:label1\" content=\"Written by\" \/>\n\t<meta name=\"twitter:data1\" content=\"Mary Todd Bergman\" \/>\n\t<meta name=\"twitter:label2\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data2\" content=\"3 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\/1412_hairclip-protein\/#article\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/1412_hairclip-protein\/\"},\"author\":{\"name\":\"Mary Todd Bergman\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/052a43af2beb3860bffa67c0f0474875\"},\"headline\":\"&#8216;Hairclip&#8217; 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