{"id":28818,"date":"2009-08-13T22:00:00","date_gmt":"2009-08-13T20:00:00","guid":{"rendered":"https:\/\/www.embl.org\/news\/?p=28818"},"modified":"2024-11-14T16:28:04","modified_gmt":"2024-11-14T15:28:04","slug":"raising-the-alarm-when-dna-goes-bad","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/raising-the-alarm-when-dna-goes-bad\/","title":{"rendered":"Raising the alarm when DNA goes bad"},"content":{"rendered":"\n<div class=\"wp-block-image\"><figure class=\"vf-figure  | vf-figure--align vf-figure--align-inline-start   size-large\"><a href=\"https:\/\/www.embl.de\/aboutus\/communication_outreach\/media_relations\/2009\/090813_Heidelberg\/ladurner_movie.mov\" target=\"_blank\" rel=\"noopener noreferrer\"><img loading=\"lazy\" decoding=\"async\" width=\"175\" height=\"107\" class=\"vf-figure__image\" src=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2020\/06\/press13aug09_s.jpg\" alt=\"\" class=\"wp-image-28832\"\/><\/a><figcaption class=\"vf-figure__caption\">Click on the picture to start the movie<br \/><strong>Macrodomain-containing proteins rapidly respond to DNA damage<br \/><\/strong>An ultraviolet laser is used to damage DNA within a human cell. The movie shows how a fluorescent version of a macrodomain-containing protein (labelled Af1521 here) rapidly accumulates at the site of DNA damage<\/figcaption><\/figure><\/div>\n\n\n\n<p>Our genome is constantly under attack from things like UV light and toxins, which can damage or even break DNA strands and ultimately lead to cancer and other diseases. Scientists have known for a long time that when DNA is damaged, a key enzyme sets off a cellular \u2018alarm bell\u2019 to alert the cell to start the repair process, but until recently little was known about how the cell detects and responds to this alarm. In a study published today in <em>Nature Structural and Molecular Biology<\/em>, researchers at the European Molecular Biology Laboratory (EMBL) in Heidelberg, Germany, have identified a whole family of proteins capable of a direct response to the alarm signal.<\/p>\n\n\n\n<p>Our genome is a huge repository of information guiding the construction and function of all the cells in our bodies. Cells sustain many hits to their DNA every day, which can lead tomutations, so they maintain a fleet of DNA repair machinery that can be rapidly mobilised and sent to damaged sites in an emergency.<\/p>\n\n\n\n<p>Because our DNA is so long and unwieldy, it needs to be packaged up with proteins and organised into a complex structure called chromatin. Scientists have known for 50 years that one component of chromatin, an enzyme known as PARP1, is activated by DNA damage and produces a molecular signal, called PAR, which raises the alarm at the site of the damage. In recent weeks, scientists have for the first time worked out how PAR is rapidly detected by the cell; in their <em>Nature Structural and Molecular Biology<\/em> paper, the group of Andreas Ladurner and their colleagues at EMBL have identified a whole family of proteins that respond to this signal by binding to it directly.<\/p>\n\n\n\n<p>What these proteins share is a special region called a macrodomain. By using a laser to reproduce DNA damage in the lab, the scientists were able to follow fluorescently-labelled macrodomain proteins in cells and observed that they quickly move to the site of DNA damage. A high-resolution image, obtained by X-ray crystallography, shows how the macrodomain forms a \u2018pocket\u2019 fitting the PAR signal exactly.<\/p>\n\n\n\n<p>Among the members of the family the researchers found a protein called histone macroH2A1.1. \u201cThis was very surprising. Histones play a major role in assembling chromatin and keeping it together, but they don\u2019t usually have macrodomains,\u201d says Ladurner. \u201cThe finding is particularly relevant, because it turns out that cancer cells don\u2019t have macroH2A1.1. The fact that one member of the rapid response team that detects DNA damage is missing could contribute to the disease.\u201d<\/p>\n\n\n\n<p>Because macroH2A1.1 is embedded in chromatin, when it recognises PAR at DNA damage sites, it drags the complex but highly-organised tangle of chromatin with it. As a result, macroH2A1.1 condenses the chromatin environment around the damaged area.<\/p>\n\n\n\n<p>The scientists are now trying to understand why this happens. One plausible explanation could be that by temporarily compacting the DNA, the broken ends of the DNA molecule are kept closer together. This should increase the chances of being able to repair it.<\/p>\n\n\n\n<p>\u201cWith these findings we\u2019ve opened up completely new perspectives to a fifty-year-old field of research,\u201d says Ladurner. \u201cWe\u2019re very excited of what lies ahead and hope that we\u2019ll soon be much closer in understanding how PARP1 and macrodomains together maintain a healthy genome.\u201d<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Our genome is constantly under attack from things like UV light and toxins, which can damage or even break DNA strands and ultimately lead to cancer and other diseases. Scientists have known for a long time that when DNA is damaged, a key enzyme sets off a cellular \u2018alarm bell\u2019 to alert the&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":[537,266,664,1748,1714],"embl_taxonomy":[9796,5146],"class_list":["post-28818","post","type-post","status-publish","format-standard","hentry","category-science","category-science-technology","tag-dna","tag-enzyme","tag-genome","tag-press-release","tag-x-ray-crystallography","embl_taxonomy-embl-heidelberg","embl_taxonomy-genome-biology"],"acf":{"vf_locked":false,"featured":true,"color":"#007B53","show_featured_image":true,"article_intro":"<h2>EMBL scientists identify a rapid response team that monitors and quickly responds to DNA damage<\/h2>\n","article_sources":[{"source_description":"<p>G. Timinszky, S. Till, P.O. Hassa, M. Hothorn, G. Kustatscher, B. Nijmeijer, J. Colombelli, M. Altmeyer, E.H.K. Stelzer, K. Scheffzek, M.O. Hottiger &#038; A.G. Ladurner. A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation. <em>Nature Structural and Molecular Biology<\/em>, 13 August 2009. DOI: 10.1038\/nsmb.1664 <\/p>\n","source_link_url":"https:\/\/www.nature.com\/articles\/nsmb.1664"}],"related_links":false,"in_this_article":false,"youtube_url":"","mp4_url":"","video_caption":"","press_contact":"EMBL Generic","translations":false},"embl_taxonomy_terms":[{"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:\"7ca3ce91-dc32-47ea-8d4b-7a53c3a3a9fd\";i:2;s:36:\"fe59a59f-fd7d-49b3-b3e4-bdd33a6642c3\";}","parents":[],"name":["Genome Biology"],"slug":"genome-biology","description":"What &gt; Research Units &gt; Genome Biology"}],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.2 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ 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