{"id":24900,"date":"2013-10-23T11:43:24","date_gmt":"2013-10-23T09:43:24","guid":{"rendered":"https:\/\/www.embl.org\/news\/?p=24900"},"modified":"2024-03-26T00:30:33","modified_gmt":"2024-03-25T23:30:33","slug":"bigger-better-faster","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/bigger-better-faster\/","title":{"rendered":"Bigger, better, faster"},"content":{"rendered":"\n<div\n  class=\"vf-box vf-box--inlay\">\n\n  <h3 class=\"vf-box__heading\">In a nutshell:<\/h3>\n  <p class=\"vf-box__text\">&#8211; High-resolution structure of RNA polymerase I determined<br \/>&#8211; Incorporates modules which prevent it from having to recruit outside help<br \/>&#8211; Can help explain the greater efficiency of this molecular machine<\/p>\n<\/div>\n\n\n\n<div class=\"wp-block-image\"><figure class=\"vf-figure  | vf-figure--align vf-figure--align-inline-start   size-medium\"><a href=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2020\/05\/131023_Heidelberg.jpg\"><img loading=\"lazy\" decoding=\"async\" width=\"300\" height=\"206\" class=\"vf-figure__image\" src=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2020\/05\/131023_Heidelberg-300x206.jpg\" alt=\"RNA polymerase\" class=\"wp-image-24902\" srcset=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2020\/05\/131023_Heidelberg-300x206.jpg 300w, https:\/\/www.embl.org\/news\/wp-content\/uploads\/2020\/05\/131023_Heidelberg.jpg 620w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/a><figcaption class=\"vf-figure__caption\">The cell\u2019s Swiss-army knife: the structure of RNA polymerase I revealed an efficiency-boosting strategy. Credit: EMBL\/C. Fe\u0301rnandez-Tornero &amp; P. Riedinger<\/figcaption><\/figure><\/div>\n\n\n\n<p>The molecular machine that makes essential components of ribosomes \u2013 the cell\u2019s protein factories \u2013 is like a Swiss-army knife, researchers at the European Molecular Biology Laboratory (EMBL) in Heidelberg, Germany, and the Centro de Investigaciones Biol\u00f3gicas in Madrid, Spain, have found. By determining the 3-dimensional structure of this machine, called RNA polymerase I, for the first time, the scientists found that it incorporates modules which prevent it from having to recruit outside help. The findings, published online today in&nbsp;<em>Nature<\/em>, can help explain why this protein works faster than its better-studied counterpart, RNA polymerase II.&nbsp;<\/p>\n\n\n\n<p>\u201cRather than recruiting certain components from outside, RNA polymerase I has them already built in, which explains why it is bigger, and less regulated, but at the same time more efficient,\u201d says\u00a0<a href=\"https:\/\/www.embl.org\/groups\/mueller\/\">Christoph M\u00fcller<\/a>\u00a0from EMBL, who led the study. \u201cBecause everything is already assembled, there\u2019s no time delay,\u201d explains Maria Moreno-Morcillo, who carried out the work.\u00a0<\/p>\n\n\n\n<p>There are three different RNA polymerases, each of which makes specific types of RNA molecule. For example, RNA polymerase II makes messenger RNA \u2013 the \u2018middle-man\u2019 that carries the information encoded in DNA to a ribosome where it can be used to make a protein. RNA polymerases I and III make parts of the machinery which reads that messenger RNA: I builds the RNA that will eventually form a ribosome, while III makes the transfer RNA that carries the protein building blocks to the ribosome for assembly. Scientists have known for over a decade what RNA polymerase II looks like and how it works, but obtaining detailed information on the structures of its counterparts has proven extremely difficult. Now that they have managed to do so for RNA polymerase I, M\u00fcller and colleagues have found explanations for some of the protein\u2019s particularities.<\/p>\n\n\n\n<p>Part of the difficulty in studying RNA polymerase I is that it is a larger molecule than RNA polymerase II. When they determined its 3-dimensional structure, the scientists found that some of the \u2018extra\u2019 modules in RNA polymerase I are remarkably similar to other, separate proteins that RNA polymerase II needs to do its job. It seems that RNA polymerase I has brought those helper modules permanently on board. In another part of the molecule, M\u00fcller and colleagues found that RNA polymerase I appears to have combined what in RNA polymerase II are two separate modules into a single, multi-tasking component. Together, these changes likely explain why RNA polymerase I can produce RNA molecules at a faster rate than RNA polymerase II.<\/p>\n\n\n\n<p>The findings also imply that the cell has fewer ways of controlling RNA polymerase I\u2019s activity, since it can\u2019t influence it by changing the availability of helper proteins as it does in the case of RNA polymerase II. But here, too, RNA polymerase I\u2019s Swiss-army knife strategy provides a solution. The structure showed that this molecular machine has a built-in regulatory mechanism: it can stop itself from attaching to DNA by bending a loop in its structure to block the space the DNA would usually dock onto.<\/p>\n\n\n\n<p>The work was carried out in collaboration with&nbsp;<a rel=\"noreferrer noopener\" href=\"http:\/\/www.cib.csic.es\/en\/grupo.php?idgrupo=72\" target=\"_blank\">Carlos Fern\u00e1ndez-Tornero<\/a>\u2019s lab at the Centro de Investigaciones Biol\u00f3gicas in Madrid, Spain, as well as researchers at the&nbsp;<a rel=\"noreferrer noopener\" href=\"http:\/\/www.uni-goettingen.de\/en\/1.html\" target=\"_blank\">University of G\u04e7ttingen<\/a>, Germany and the&nbsp;<a rel=\"noreferrer noopener\" href=\"http:\/\/www.synchrotron-soleil.fr\/\" target=\"_blank\">SOLEIL synchrotron<\/a>&nbsp;in France, where some of the structural data was obtained. Structural data was also obtained at the&nbsp;<a rel=\"noreferrer noopener\" href=\"http:\/\/www.desy.de\/research\/facilities\/petra_iii\/index_eng.html\" target=\"_blank\">Petra III<\/a>&nbsp;ring at EMBL Hamburg, on the DESY campus in Germany.<\/p>\n\n\n\n<p>Christoph M\u00fcller recently received an Advanced Grant from the European Research Council (ERC) to study RNA polymerase I and the proteins it interacts with.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>The molecular machine that makes essential components of ribosomes \u2013 the cell\u2019s protein factories \u2013 is like a Swiss-army knife, researchers at the European Molecular Biology Laboratory (EMBL) in Heidelberg, Germany, and the Centro de Investigaciones Biol\u00f3gicas in Madrid, Spain, have found.&hellip;<\/p>\n","protected":false},"author":16,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[543,657,70],"embl_taxonomy":[],"class_list":["post-24900","post","type-post","status-publish","format-standard","hentry","category-science","category-science-technology","tag-erc-grant","tag-polymerase","tag-rna"],"acf":{"show_featured_image":false,"vf_locked":false,"featured":false,"article_intro":"<p>3D structure reveals protein\u2019s Swiss-army knife strategy<\/p>\n","article_sources":[{"source_description":"<p>Fern\u00e1ndez-Tornero, C., Moreno-Morcillo, M., Rashid, U.J., Taylor, N.M.I, Ruiz, F.M., Gruene, T., Legrand, P., Steuerwald, U. &#038; M\u00fcller, C.W. Crystal structure of the 14-subunit RNA polymerase I. Published online in <em>Nature<\/em> on 23 October 2013. DOI: 10.1038\/nature12636.<\/p>\n","source_link_url":"http:\/\/dx.doi.org\/10.1038\/nature12636"}],"related_links":false,"in_this_article":false,"color":"#007B53","youtube_url":"","mp4_url":"","video_caption":"","press_contact":"EMBL Generic","field_target_display":"embl","source_article":false},"embl_taxonomy_terms":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.2 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>Bigger, better, faster | EMBL<\/title>\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\/bigger-better-faster\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Bigger, better, faster | EMBL\" \/>\n<meta property=\"og:description\" content=\"The molecular machine that makes essential components of ribosomes \u2013 the cell\u2019s protein factories \u2013 is like a Swiss-army knife, researchers at the European Molecular Biology Laboratory (EMBL) in Heidelberg, Germany, and the Centro de Investigaciones Biol\u00f3gicas in Madrid, Spain, have found.&hellip;\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.embl.org\/news\/science\/bigger-better-faster\/\" \/>\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=\"2013-10-23T09:43:24+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2024-03-25T23:30:33+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2020\/05\/131023_Heidelberg-300x206.jpg\" \/>\n<meta name=\"author\" content=\"Guest author(s)\" \/>\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=\"Guest author(s)\" \/>\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\/bigger-better-faster\/#article\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/bigger-better-faster\/\"},\"author\":{\"name\":\"Guest author(s)\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/b4d9366b2ebe691c4015c64c3619205b\"},\"headline\":\"Bigger, better, faster\",\"datePublished\":\"2013-10-23T09:43:24+00:00\",\"dateModified\":\"2024-03-25T23:30:33+00:00\",\"mainEntityOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/bigger-better-faster\/\"},\"wordCount\":637,\"publisher\":{\"@id\":\"https:\/\/www.embl.org\/news\/#organization\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/bigger-better-faster\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2020\/05\/131023_Heidelberg-300x206.jpg\",\"keywords\":[\"erc grant\",\"polymerase\",\"rna\"],\"articleSection\":[\"Science\",\"Science &amp; Technology\"],\"inLanguage\":\"en-US\"},{\"@type\":\"WebPage\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/bigger-better-faster\/\",\"url\":\"https:\/\/www.embl.org\/news\/science\/bigger-better-faster\/\",\"name\":\"Bigger, better, faster | EMBL\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/#website\"},\"primaryImageOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/bigger-better-faster\/#primaryimage\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/bigger-better-faster\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2020\/05\/131023_Heidelberg-300x206.jpg\",\"datePublished\":\"2013-10-23T09:43:24+00:00\",\"dateModified\":\"2024-03-25T23:30:33+00:00\",\"inLanguage\":\"en-US\",\"potentialAction\":[{\"@type\":\"ReadAction\",\"target\":[\"https:\/\/www.embl.org\/news\/science\/bigger-better-faster\/\"]}]},{\"@type\":\"ImageObject\",\"inLanguage\":\"en-US\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/bigger-better-faster\/#primaryimage\",\"url\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2020\/05\/131023_Heidelberg.jpg\",\"contentUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2020\/05\/131023_Heidelberg.jpg\",\"width\":620,\"height\":425,\"caption\":\"The cell\u2019s Swiss-army knife: the structure of RNA polymerase I revealed an efficiency-boosting strategy. 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