Detailed view of a crucial enzymatic complex revealed

Nov 07, 2011
Detailed view of a crucial enzymatic complex revealed
Model of the large subunit of the ribosome from a higher organism (Photograph: Katharina Bohm, Felix Voigts-Hoffmann / ETH Zürich)

Researchers led by ETH professor Nenad Ban have now completed the three-dimensional structure of the ribosome from a higher organism. This structure will increase the understanding of this cellular “protein factory” and facilitate the development of novel drugs.

The machinery that reads genetic information within a cell and translates it into corresponding proteins, the so-called , is among the most complex cellular enzymes known in biology. It has been studied for decades. Ten years ago, scientists have solved the first three-dimensional of this complex from prokaryotes (ie. bacteria). They were awarded with the Nobel Prize in Chemistry in 2009.

In higher such as fungi, plants and animals (so-called eukaryotes), the ribosome is even more complex than in bacteria. Researchers led by Nenad Ban, professor at the Institute for Molecular Biology and Biophysics at ETH Zurich have now solved the three-dimensional structure of the larger of two ribosomal subunits from a higher organism, the single-celled ciliate Tetrahymena thermophila. This ribosome is akin to the ones of multi-cellular organisms such as humans. The scientists published their work today in the magazine Science. Researchers of the same group at ETH Zurich had already published the structure of the smaller ribosomal subunit of the ciliate earlier this year.

Towards a better understanding of the ribosomal function

Comparing the ribosomal structures of both, bacteria and higher organisms, will enable scientists to develop novel specific pharmaceutical compounds against pathogens and pests. Among these could be antibiotics and fungicides. Furthermore, the findings could lead to the development of novel antiviral drugs since many viruses need to bind to and manipulate the ribosomes of their host cells in order to replicate.

The newly revealed structure could furthermore help to better understand the initiation of protein synthesis and to gain insights into the evolutionary development of the ribosomes of higher organisms.

Ribosomes of higher organisms have been a major focus at the laboratory of Prof. Ban since 2001. The work of the scientists at ETH Zurich was supported by the National Centre of Excellence in Research (NCCR) in Structural Biology of the Swiss National Science Foundation. Data used for structure determination was collected at the Swiss Light Source.

Explore further: Fighting bacteria—with viruses

More information: Klinge S, Voigts-Hoffmann F, Leibundgut M, Arpagaus S, Ban N: Crystal Structure of the Eukaryotic 60S Ribosomal Subunit in Complex with Initiation Factor 6. Science.

Related Stories

The eukaryotic ribosome unveils its structure

Dec 01, 2010

One year after the Nobel Prize in chemistry was awarded for the discovery of the bacterial ribosome's atomic structure, French researchers from the Institut de Genetique et de Biologie Moleculaire et Cellulaire ...

Biologists probe the machinery of cellular protein factories

Sep 13, 2006

Proteins of all sizes and shapes do most of the work in living cells, and the DNA sequences in genes spell out the instructions for making those proteins. The crucial job of reading the genetic instructions and synthesizing ...

Recommended for you

Fighting bacteria—with viruses

Jul 24, 2014

Research published today in PLOS Pathogens reveals how viruses called bacteriophages destroy the bacterium Clostridium difficile (C. diff), which is becoming a serious problem in hospitals and healthcare institutes, due to its re ...

Atomic structure of key muscle component revealed

Jul 24, 2014

Actin is the most abundant protein in the body, and when you look more closely at its fundamental role in life, it's easy to see why. It is the basis of most movement in the body, and all cells and components ...

Brand new technology detects probiotic organisms in food

Jul 23, 2014

In the food industr, ity is very important to ensure the quality and safety of products consumed by the population to improve their properties and reduce foodborne illness. Therefore, a team of Mexican researchers ...

Protein evolution follows a modular principle

Jul 23, 2014

Proteins impart shape and stability to cells, drive metabolic processes and transmit signals. To perform these manifold tasks, they fold into complex three-dimensional shapes. Scientists at the Max Planck ...

Report on viruses looks beyond disease

Jul 22, 2014

In contrast to their negative reputation as disease causing agents, some viruses can perform crucial biological and evolutionary functions that help to shape the world we live in today, according to a new report by the American ...

User comments : 0