STOCKHOLM (Reuters) - Three scientists who produced atom-by-atom maps of the mysterious, life-giving ribosome won the Nobel chemistry prize on Wednesday for a breakthrough that has allowed researchers to develop powerful new antibiotics.
While DNA molecules contain the blueprint for life inside each cell of every organism, it is the ribosome that translates that information into life.
Israeli Ada Yonath and Americans Venkatraman Ramakrishnan and Thomas Steitz shared the 10 million Swedish crown ($1.4 million) prize for showing how the ribosome, a kind of protein factory, operates at the atomic level.
“As ribosomes are crucial to life, they are also a major target for new antibiotics,” the Nobel Committee for Chemistry at the Royal Swedish Academy of Sciences said in a statement.
The academy said many of today’s antibiotics cure various diseases by blocking the function of bacterial ribosomes.
Yonath, a professor at the Weizmann Institute of Science in Israel, told a news conference by telephone that she was elated to receive the award: “It is above and beyond my dreams.”
A method known as X-ray crystallography was used to pinpoint each of the hundreds of thousands of atoms in a ribosome.
The technique involves aiming X-rays at a crystal. The rays scatter when they hit atoms and by looking at how they spread out, scientists can determine where atoms are positioned.
Yonath made the initial breakthrough at the end of the 1970s when she first tried the method on the ribosome -- a feat most considered impossible.
LIFE IN THE DEAD SEA
Yonath started by taking a micro-organism found in the nearby Dead Sea and crystallizing its ribosomes. She did this by freezing them at nearly minus 200 degrees Celsius.
Jeremy Berg, director of the U.S. National Institute of General Medical Sciences which funded the work of all three researchers, said he was amazed at how intrepid Yonath was.
“I remember at the time being just completely stunned that she was somewhere between brave enough and crazy enough because it was way, way, way beyond the technology available at that point,” he told Reuters.
But it would take another 20 years before a full map could be made. During that time, two others joined the race: Yale University’s Steitz and Indian-born Ramakrishnan of the MRC Laboratory of Molecular Biology in Britain.
In 1998, Steitz published the first crystal structure of a large part of a ribosome, something that looked like a dim photograph. The three scientists reached the finish line almost simultaneously in 2000, publishing crystal structures that were sharply enough defined to locate atoms.
Steitz, whose PhD advisor William Lipscomb captured the 1976 prize for chemistry, told Reuters by phone from his office in Connecticut that he received a “nice wake-up call” at 5:30 a.m. “I’m very excited of course,” he said. “It’s so nice to be appreciated.”
Steitz now wants to go beyond still images of the ribosome. He is trying to make a movie to capture every step of the process. Asked whether the award will change his life, he said he expected it would. “But it won’t change what I want to do.”
Ramakrishnan paid tribute to those who worked beside him.
“I have to say that I am deeply indebted to all of the brilliant associates, students and post docs who worked in my lab as science is a highly collaborative enterprise,” he said in a statement.
Scientists use ribosome models to develop antibiotics that can fight harmful bacteria, but many believe researchers have only just begun to tap into the potential these models offer.
“Fifty percent of all antibiotics target the ribosome, and now we have the tools to begin looking at if there are other substances we can fit into different slots to block and disturb bacteria in our bodies,” said Peter Brezinski, a member of the chemistry panel at the Royal Academy of Sciences in Stockholm.
Prizes for the sciences and for peace were established in the will of 19th century dynamite tycoon Alfred Nobel and have been handed out since 1901. Sweden’s central bank began awarding a prize for economics in 1969.
Wednesday’s award was the second protein-related prize in a row. Last year’s chemistry Nobel went to researchers for the discovery of a glowing jellyfish protein that makes cells, tissues and even organs light up.
Previous winners have included Marie Curie, who won the 1911 prize and is remembered for her contribution to the fight against cancer, and Frederick Sanger, who won the 1958 prize for his work on the structure of proteins, especially insulin.
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