{"id":4606,"date":"2015-07-16T18:00:40","date_gmt":"2015-07-16T16:00:40","guid":{"rendered":"http:\/\/news.embl.de\/?p=4606"},"modified":"2024-04-19T15:11:21","modified_gmt":"2024-04-19T13:11:21","slug":"1507-oskar","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/1507-oskar\/","title":{"rendered":"Oskar\u2019s structure revealed"},"content":{"rendered":"\n<p>This advance \u2013 published today in <i>Cell Reports \u2013 <\/i>has also enabled the team to gather the first insights into how this poorly understood protein functions. The research was carried out with fruit flies, but has implications for other animals, as many organisms, including humans, also have part of the Oskar protein.<\/p>\n\n\n\n<p>Named after the main character from G\u00fcnter Grass\u2019 novel <i>The Tin Drum,<\/i> who chose never to grow up, the Oskar protein is essential for development. Embryos that develop from fruit fly eggs lacking the normal amount of Oskar protein are unable to form germ cells \u2013 cells that allow reproduction \u2013 and so the resulting flies are sterile. Complete lack of the Oskar protein also prevents the embryo\u2019s abdomen from forming normally which stunts its growth so it dies.<\/p>\n\n\n\n<p>In a healthy egg Oskar initiates the formation of what\u2019s known as the germ plasm \u2013 a gathering of proteins and RNAs within the cytoplasm, which then goes on to form a new germ cell. Germ plasm normally forms in a particular position within the egg, but if Oskar is artificially moved elsewhere, the germ plasm will form in the new location.<\/p>\n\n\n\n<blockquote class=\"vf-blockquote\"><p>Solving the structure has enabled us to start to see how the different parts of the protein function at a molecular level.<\/p><\/blockquote>\n\n\n\n<p>Co-author of the paper, <a title=\"Ephrussi group\" href=\"http:\/\/www.embl.de\/research\/units\/dev_biology\/ephrussi\/index.html\" target=\"_blank\" rel=\"noopener noreferrer\">Anne Ephrussi<\/a> said: \u201cWhile we\u2019ve known Oskar\u2019s genetic role in development for some time, we\u2019ve not known the mechanism by which this takes place. Solving the structure has enabled us to start to see how the different parts of the protein function at a molecular level, which could help us to understand more about this stage of development in a wide range of organisms.\u201d<\/p>\n\n\n\n<p>Using X-ray crystallography, carried out in collaboration with the lab of <a href=\"http:\/\/www.embl.de\/research\/units\/scb\/mueller_christoph\/index.html\" target=\"_blank\" rel=\"noopener noreferrer\">Christoph M\u00fcller<\/a>, the team was able to determine for the first time the structure of Oskar\u2019s two domains, called OSK and LOTUS. The OSK domain is found in some insects, including the fruit fly and the mosquito. The LOTUS domain is more widespread, being found in bacteria, plants and animals, including mice and in humans.<\/p>\n\n\n\n<p>Using experiments with fruit fly eggs, the team saw that Oskar binds to RNA within the cell \u2013 specifically three RNAs derived from genes also known to be important to germline development. But when they looked in more detail, they found that it was only the OSK domain that binds to RNA.<\/p>\n\n\n\n<p>The LOTUS domain \u2013 which they expected to bind to RNA \u2013 didn\u2019t in fact do so. Instead, the team found that LOTUS binds to an enzyme called Vasa helicase, which is also one of the essential initial ingredients of the germ plasm.<\/p>\n\n\n\n<blockquote class=\"vf-blockquote\"><p>It could be that this interaction isn\u2019t specific to the fruit fly but also takes place in other germline cells.<\/p><\/blockquote>\n\n\n\n<p>\u201cVasa, like LOTUS, is widely found in other organisms, including animals, so it could be that this interaction isn\u2019t specific to the fruit fly but also takes place in other germline cells,\u201d says co-researcher, Mandy Jeske. \u201cThere is still much to learn about how the Oskar protein functions \u2013&nbsp;for example we don\u2019t know yet if LOTUS just binds to Vasa or if it also controls Vasa\u2019s activity. This work has opened up lots of exciting new avenues for investigation.\u201d<\/p>\n","protected":false},"excerpt":{"rendered":"<p>3D structure of Oskar protein gives first molecular insight into how it functions.<\/p>\n","protected":false},"author":25,"featured_media":4608,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[29,55,357,43,1748,35],"embl_taxonomy":[18861,9796,19341],"class_list":["post-4606","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-crystallography","tag-development","tag-ephrussi","tag-heidelberg","tag-press-release","tag-structural-biology","embl_taxonomy-christoph-muller","embl_taxonomy-embl-heidelberg","embl_taxonomy-muller-group"],"acf":{"article_intro":"<p>The structure of two parts of the Oskar protein, known to be essential for the development of reproductive cells, has been solved by scientists from EMBL Heidelberg.<\/p>\n","related_links":[{"link_description":"This article first appeared as a press release on the EMBL website, 16 July 2015","link_url":"http:\/\/www.embl.org\/press\/2015\/150716_Ephrussi"}],"article_sources":[{"source_description":"<p>Jeske, Bordi, Glatt<em> <i>et al. Cell Reports<\/i>. 16 July 2015.<\/em> DOI:10.1016\/j.celrep.2015.06.055<\/p>\n","source_link_url":"http:\/\/dx.doi.org\/10.1016\/j.celrep.2015.06.055"}],"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":"EMBL Generic","source_article":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 &gt; 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 &gt; All EMBL sites &gt; EMBL Heidelberg"},{"uuid":"a:3:{i:0;s:36:\"302cfdf7-365b-462a-be65-82c7b783ebf7\";i:1;s:36:\"bd910dd7-0cda-4618-8bfa-d37fbda8438e\";i:2;s:36:\"9e7c6e04-1ed3-45c2-a25a-6ad53d702521\";}","parents":[],"name":["M\u00fcller Group"],"slug":"muller-group","description":"What &gt; Molecular Systems Biology &gt; M\u00fcller Group"}],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.2 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>Oskar\u2019s structure revealed | EMBL<\/title>\n<meta name=\"description\" content=\"3D structure of Oskar protein gives first molecular insight into how it functions.\" \/>\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\/1507-oskar\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Oskar\u2019s structure revealed | EMBL\" \/>\n<meta property=\"og:description\" content=\"3D structure of Oskar protein gives first molecular insight into how it functions.\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.embl.org\/news\/science\/1507-oskar\/\" \/>\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=\"2015-07-16T16:00:40+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2024-04-19T13:11:21+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2015\/07\/1507_ephrussi-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=\"Isabelle Kling\" \/>\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=\"Isabelle Kling\" \/>\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\/1507-oskar\/#article\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/1507-oskar\/\"},\"author\":{\"name\":\"Isabelle Kling\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/e0df3d2a7d51e01a8118c494997b85c3\"},\"headline\":\"Oskar\u2019s structure revealed\",\"datePublished\":\"2015-07-16T16:00:40+00:00\",\"dateModified\":\"2024-04-19T13:11:21+00:00\",\"mainEntityOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/1507-oskar\/\"},\"wordCount\":553,\"publisher\":{\"@id\":\"https:\/\/www.embl.org\/news\/#organization\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/1507-oskar\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2015\/07\/1507_ephrussi-ib.jpg\",\"keywords\":[\"crystallography\",\"development\",\"ephrussi\",\"heidelberg\",\"press release\",\"structural biology\"],\"articleSection\":[\"Science\",\"Science &amp; 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