ChemPhysChem

Cover image for Vol. 18 Issue 15

Editor: Greta Heydenrych; Editorial Board Chairs: Christian Amatore, Michael Grätzel, Michel Orrit

Impact Factor: 3.075

ISI Journal Citation Reports © Ranking: 2016: 8/35 (Physics Atomic Molecular & Chemical); 54/145 (Chemistry Physical)

Online ISSN: 1439-7641

Associated Title(s): Advanced Materials, ChemBioChem, ChemCatChem, ChemElectroChem, ChemPhotoChem, ChemSusChem, Small

October 07, 2009

2009 Chemistry Nobel Prize for Studies of the Ribosome

2009 Chemistry Nobel Prize for Studies of the RibosomeThe 2009 Nobel Prize in Chemistry has been awarded to the two US scientists Venkatraman Ramakrishnan (currently working in UK and born in India) and Thomas A. Steitz and the Israeli researcher Ada E. Yonath "for studies of the structure and function of the ribosome." The three Laureates are rewarded for mapping this enzyme –one of the cell's most complex machineries– at the atomic level. By using X-ray crystallography, the researchers were able to show us what the ribosome looks like and how it functions at the atomic level.

"The ribosome is the machinery which connects the nucleic acid world and the protein world", says 1988 Nobel Laureate Hartmut Michel of the Max Planck Institute of Biophysics, who is an expert in proteins and X-ray crystallography. "It translates the genetic information into specific proteins and is therefore one of the most fundamental machineries of life." The ribosome reads the information in messenger RNA, and based upon that information, it produces protein. The body contains tens of thousands of different proteins that work with an amazing precision, controlling biological processes at the chemical level.

"Roughly half the dry weight of any organism is protein, and the ribosome is the enzyme that makes protein", says Peter Moore, Sterling Professor of Chemistry at Yale University, who has been studying the ribosome for many years. He explains that ribosome is an unusual enzyme in being mostly of RNA. This makes it extremely interesting biochemically, he says. "Both because of its chemistry and because of the importance of its role in the cell". According to Norbert Polacek, Assistant Professor at the Innsbruck Biocenter/Division of Genomics and RNomics, the work carried out by the Nobel Laureates also has a major impact on the evolutionary theory. The detailed structures determined by them "support the idea that life on earth began as an 'RNA world', in which RNA enzymes (such as the ribosome) catalyzed all biologically relevant chemical reactions", he says.

Understanding how the ribosome works has led to a better scientific explanation of life at the atomic level, but this knowledge has also provided insights into how to save lives and can be used, for example, in the fight against antibiotic-resistant bacteria (e.g. MRSA, methicillin-resistant Staphylococcus aureus). The ribosome is the target of many antibiotics. However, bacteria have become resistant to many of these drugs at a threatening rate. Today, the structure of the ribosome is known in detail so that antibiotics that will attack drug-resistant bacteria can be created by structure-based drug design. This year's three Nobel Laureates in chemistry have all produced 3D structures that show how different antibiotics bind to the ribosome. Several companies are now using the structures of the ribosome to develop new antibiotics.

Ada E. Yonath, who is a member of the Editorial Advisory Board of our sister journal ChemBioChem, will speak –along with three fellow Nobel Laureates and other high-ranking scientists– at our 10th anniversary symposium in Paris next May.

Kira Welter

Image: Nobel Medal (© ® The Nobel Foundation).


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