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Choreographed origami: folding ribosomal RNA involves paired tagging sequence. 13 October 2013

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Choreographed origami: folding ribosomal RNA involves paired tagging sequence. 13 October 2013

One important step in building ribosomes – the cell’s protein factories – is like a strictly choreographed dance, scientists at the European Molecular Biology Laboratory (EMBL) in Heidelberg, Germany, have discovered. To build these factories, other ‘machines’ inside the cell have to produce specific RNA molecules and fold them into the right shape, then combine the folded RNA with proteins to form a working ribosome. Like a budding origami artist pencilling in the folds, the cell uses tags called methyl groups to help mark where and how an RNA molecule should be folded. In work published online today in Nature, the scientists have discovered that pairs of these tags are added in a specific order. The study combined nuclear magnetic resonance experiments performed at EMBL and neutron scattering experiments performed at the ILL in Grenoble, France.

Led by Teresa Carlomagno at EMBL, the scientists were able to determine the 3D structure of the complex that adds methyl tags to the RNA. They discovered that the different components of this tagging machine pair up and move in sequence, like dancers following a set choreography.
“We found that the complex has four copies of each protein, and four methylation sites on the RNA, but these methylation sites aren’t all the same,” Carlomagno says. “They come in pairs, and one pair has to be methylated before the other.”

The fact that the pairs of tags have to be added in a particular order could be a way for the cell to control how the RNA is folded, and ultimately when and where ribosomes are formed, the scientists believe.

The study provides a detailed view of the complex in a form that is very close to what is found inside our cells. To obtain their results, the EMBL scientists teamed up with Frank Gabel from the Institut de Biologie Structurale (IBS) and the Institut Laue-Langevin (ILL), the world’s flagship centre for neutron science in Grenoble, France, to combine their expertise in nuclear magnetic resonance (NMR) with small-angle neutron scattering (SANS).

At the ILL the neutron analysis techniques were enhanced through a biochemical trick known as contrast variation by which the hydrogen in a molecule is exchanged for its heavier isotope deuterium in order to distinguish it more clearly against the background of the surrounding solvent. Using this technique, the EMBL team were able to follow the individual sub-units, including twelve protein partners and two RNA structures, throughout these complexes.

“This type of small-angle neutron scattering at low angles is perfect for investigating the structure of relatively large biomacromolecular complexes as well as the proteins that make them up,” Gabel says. “In fact it was the pioneering of these techniques in the field of biology here at the ILL in the 1970s and 80s that contributed to the first detailed investigation of ribosome molecules over 30 years ago. The ILL’s dedication to supporting the biological sciences continues today and the combination of our neutron techniques with world leading NMR groups like EMBL’s provides today’s biologists with a cutting-edge tool for investigating the structure and behaviour of life’s building blocks.”

Re.: Nature, 13 October 2013. DOI:10.1038/nature12581

Contact:James Romero  +44 8456801866

Notes to editors

About ILL – The Institut Laue-Langevin (ILL) is an international research centre based in Grenoble, France. It has led the world in neutron-scattering science and technology for almost 40 years, since experiments began in 1972. ILL operates one of the most intense neutron sources in the world, feeding beams of neutrons to a suite of 40 high-performance instruments that are constantly upgraded. Each year 1,200 researchers from over 40 countries visit ILL to conduct research into condensed matter physics, (green) chemistry, biology, nuclear physics, and materials science. The UK, along with France and Germany is an associate and major funder of the ILL.

About EMBL - The European Molecular Biology Laboratory is a basic research institute funded by public research monies from 20 member states (Austria, Belgium, Croatia, Denmark, Finland, France, Germany, Greece, Iceland, Ireland, Israel, Italy, Luxembourg, the Netherlands, Norway, Portugal, Spain, Sweden, Switzerland and the United Kingdom) and associate member state Australia. Research at EMBL is conducted by approximately 85 independent groups covering the spectrum of molecular biology. The Laboratory has five units: the main Laboratory in Heidelberg, and Outstations in Hinxton (the European Bioinformatics Institute), Grenoble, Hamburg, and Monterotondo near Rome. The cornerstones of EMBL’s mission are: to perform basic research in molecular biology; to train scientists, students and visitors at all levels; to offer vital services to scientists in the member states; to develop new instruments and methods in the life sciences and to actively engage in technology transfer activities. Around 190 students are enrolled in EMBL’s International PhD programme. Additionally, the Laboratory offers a platform for dialogue with the general public through various science communication activities such as lecture series, visitor programmes and the dissemination of scientific achievements.

About IBS - The Institut de Biologie Structurale Jean-Pierre Ebel (IBS) is a French research institute jointly operated by the Atomic Energy Commission (CEA), the National Center for Scientific Research (CNRS), and the University Joseph Fourier in Grenoble. The IBS hosts 15 independent groups (240 staff) performing interdisciplinary research at the interface of biology, physics and chemistry. In 2002 the IBS, EMBL and two other European institutes (the European Synchrotron Radiation Facility and the Institut Laue-Langevin) formed the Partnership for Structural Biology, whose primary objective is to study the structure and function of proteins and other biomolecules, particularly those involved in human disease.