Trapped in a ring: Ring-like protein complex helps ensure accurate protein production

Feb 21, 2012

In fairy tales, magic rings endow their owners with special abilities: the ring makes the wearer invisible, fulfils his wishes, or otherwise helps the hero on the path to his destiny. Similarly, a ring-like structure found in a protein complex called 'Elongator' has led researchers at the European Molecular Biology Laboratory (EMBL) in Heidelberg, Germany, and the Institut de Génétique et Biologie Moléculaire et Cellulaire (IGBMC) in Strasbourg, France, in exciting new directions. Published today in Nature Structural & Molecular Biology, the first three-dimensional structure of part of this complex provides new clues to its tasks inside the cell and to its role in neurodegenerative diseases.

Changes to the proteins that make up Elongator have been linked to disorders such as familial dysautonomia and childhood epilepsy, and scientists knew that the complex is involved in a variety of processes inside the cell, but exactly what it does has so far remained a mystery.

Elongator is composed of 6 different proteins. Scientists in Christoph Müller's lab at EMBL and Bertrand Séraphin's lab at IGBMC looked at three of these proteins, which are known to work together. They discovered that, instead of just clumping together as a trio, these proteins team up in two identical trios to form a ring. This unexpected structure sparked new thoughts. It suggested that the ring's job in the Elongator complex might be similar to that of other complexes, called helicases, which use ring-like structures made out of six copies of the same protein to bind to DNA or RNA.

The researchers found only one molecule that slots into Elongator's ring: tRNA. tRNA transports amino acids to the 'factories' in the cell where they will be stitched together into a protein according to the instructions spelled out in the cell's DNA. It seems that Elongator's protein ring holds the tRNA in place while other parts of the Elongator complex work on it, introducing a chemical modification which ultimately ensures that the DNA is accurately converted into protein. The findings also suggest that, once work on the tRNA is complete, a different molecule, ATP, is broken down on the outer margin of the . This, the scientists believe, would subtly alter the shape of the ring's proteins, releasing the tRNA and allowing the whole process to start again.

Next, Müller, Séraphin and colleagues would like to investigate what tools and tricks other parts of Elongator employ to help the whole complex perform its tasks inside the cell.

Explore further: Students create microbe to weaken superbug

add to favorites email to friend print save as pdf

Related Stories

New compound effectively treats fungal infections

Jun 22, 2007

A new mechanism to attack hard-to-treat fungal infections has been revealed by scientists from the biotech company Anacor Pharmaceuticals Inc., California, and the European Molecular Biology Laboratory (EMBL) outstation in ...

Biologists uncover a novel cellular proofreading mechanism

Nov 11, 2011

(PhysOrg.com) -- To make proteins, cells assemble long chains of amino acids, based on genetic instructions from DNA. That construction takes place in a tiny cellular structure called a ribosome, to which amino acids are ...

Recommended for you

Students create microbe to weaken superbug

5 hours ago

A team of undergraduate students from the University of Waterloo have designed a synthetic organism that may one day help doctors treat MRSA, an antibiotic-resistant superbug.

Body size requires hormones under control

13 hours ago

The proper regulation of body size is of fundamental importance, but the mechanisms that stop growth are still unclear. In a study now published in the scientific journal eLife, a research group from Instit ...

User comments : 0

Please sign in to add a comment. Registration is free, and takes less than a minute. Read more

Click here to reset your password.
Sign in to get notified via email when new comments are made.