Pioneering protein work behind pair's US$1m prize

PUBLISHED : Sunday, 03 June, 2012, 12:00am
UPDATED : Sunday, 03 June, 2012, 12:00am
 

Two scientists who have spotted 'chaperones', the proteins that perform quality control in the formation of new proteins within cells, are winners of this year's Shaw Prize for life science and medicine.

Professor Franz-Ulrich Hartl, director of the Max Planck Institute of Biochemistry in Martinsried, Germany, and professor Arthur Horwich, of Yale University, will collect their US$1 million prize in Hong Kong in September.

Their work was 'very, very important' because it helps scientists explain what goes wrong in the formation of new proteins in diseases such as Alzheimer's and Huntington's, said Kenneth Young, vice-chairman of the Shaw Prize board of adjudicators.

'Scientists haven't yet found a way to cure, for example, Alzheimer's disease, and their work has brought us closer to finding it,' said Young, who is also a physics professor at Chinese University.

A protein begins its life as a long chain of amino acids that is eventually folded, and how it is folded can have very different effects on our health.

Protein misfolding can cause diseases such as Alzheimer's and Huntington's and some forms of cancer.

When proteins misfold, they clump together. These clumps can often gather in the brain, where they are believed to cause the symptoms of such diseases. Some proteins fold spontaneously in the test tube, yet others require protein 'chaperones' to guide folding in intact cells and in the test tube. Hartl and Horwich began working together in 1989 and identified the 'chaperones' responsible for mediating such folding, though they later worked separately.

They also showed, atom by atom, the exact geometry of the action of a chaperone, called GroE, in the test tube and later through detailed inspection. In separate contributions, they showed that GroE captures an unfolded polypeptide - a group of amino acids - in a closed chamber that changes its shape in stages until the folded protein is released as a finished product. In order to carry out their function, for instance as enzymes or antibodies, they must take on a particular shape.

Now researchers in the field are talking about dealing with viruses, bacteria and infectious diseases by inhibiting chaperones. They are also thinking of boosting chaperone function to help treat diseases because drugs that inhibit the function of these proteins can help other proteins in the body to fold.

The duo received the Albert Lasker Basic Medical Research Award last year for discovering a cellular machine that controls how newly manufactured proteins fold into their biologically active structures.

Other winners include Professor David Jewitt of the University of California, Los Angeles, and Jane Luu, from the Massachusetts Institute of Technology, who share the Shaw Prize for astronomy. The prize for mathematical sciences is awarded to Professor Maxim Kontsevich, of L'Institut des Hautes ?tudes Scientifique in France, for his work in algebra, geometry and mathematical physics.

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