Nobel Honors Works on Telomeres and Ribosome
October 9, 2009 |
Three scientists from the United States, Elizabeth H. Blackburn, Carol W. Greider and Jack W. Szostak, won the 2009 Nobel Prize for Physiology or Medicine for their discovery "of how chromosomes are protected by telomeres and the enzyme telomerase." Blackburn and colleagues solved a fundamental problem in cell division: how chromosomes are copied faithfully during the process and how they are protected from degradation. Telomeres are regions at the end of chromosomes that prevent DNA strands from unraveling. They are akin to the plastic tips at the end of shoelaces. The scientists showed that cells age if the telomeres are shortened. They also discovered an enzyme, which they called telomerase, that allows for replacement of telomeres. The discovery of telomerase has stimulated the development of new therapeutic strategies to combat cancer and inherited diseases caused by defective telomerase like aplastic anemia.
The Nobel Prize Committee in a press release noted that "the discoveries by Blackburn, Greider and Szostak have added a new dimension to our understanding of the cell, shed light on disease mechanisms, and stimulated the development of potential new therapies."
The Nobel Prize Committee at the Karolinska Institute has also announced the 2009 prize for chemistry. The award went to Americans Venkatraman Ramakrishnan and Thomas Steitz and Israeli Ada Yonath for their work on an atomic scale map of the ribosome, the cell's protein-making factory. Yonath produced the first X ray crystallographic images of the ribosome structure in the 1970s, a task the Nobel committee said was then considered impossible. Steitz and Ramakrishnan, on the other hand, worked to determine the atomic structures of the ribosome's 50S and 30S subunits.
"An understanding of the ribosome's innermost workings is important for a scientific understanding of life. This knowledge can be put to a practical and immediate use; many of today's antibiotics cure various diseases by blocking the function of bacterial ribosomes," the committee pointed out in a press release.
The press releases are available at http://nobelprize.org/nobel_prizes/medicine/laureates/2009/press.html and http://nobelprize.org/nobel_prizes/chemistry/laureates/2009/press.html
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