A version of this article appeared in print on October 9, 2008, on page A25 of the New York edition.

October 9, 2008

Three Chemists Win Nobel Prize

By KENNETH CHANG

One Japanese and two American scientists have won this year’s Nobel Prize in Chemistry for taking the ability of some jellyfish to glow and transforming it into a ubiquitous tool of molecular biology for watching the dance of living cells and the proteins within them.

The fluorescent proteins are now routinely used for observing the growth and fate of specific cells like nerve cells damaged during Alzheimer’s disease.

The winners are Osamu Shimomura, 80, an emeritus professor at the Marine Biological Laboratory in Woods Hole, Mass., and Boston University Medical School; Martin Chalfie, 61, a professor of biological sciences at Columbia University; and Roger Y. Tsien, 56, a professor of pharmacology at the University of California, San Diego.

Each will receive a third of the 10 million krona prize (about $1.4 million) awarded by the Royal Swedish Academy of Sciences.

Dr. Shimomura said he received a 5 a.m. phone call informing him he was a Nobelist. “The reaction was just surprise,” he said.

Dr. Tsien was not caught completely unaware. Last week, the Thomson Reuters news service listed him among its predictions for this year’s Nobel Prize winners. “I didn’t want to put any credence in it,” Dr. Tsien said, noting that the predictions for the physics and medicine prizes this week were wrong.

Dr. Tsien (pronounced chen) added that his work was “only one little piece” amid the work of many. “It wasn’t necessarily the case they had to give it to me,” he said. “Obviously, it’s pretty nice to hear.”

Dr. Chalfie never received the phone call from Sweden. “I slept through it,” he acknowledged at a news conference at Columbia. He said he had inadvertently turned down the ringer on his telephone a couple of days ago. He woke up at 6:10 in the morning and thought the soft ring was coming from a neighboring apartment.

“I was a little bit annoyed that they weren’t answering their phone,” he said. “I then realized because it was after 6, that they must have announced the Nobel Prize in Chemistry. I decided to find out who the schnook was that won it this year. So I opened up my laptop and found out I was the schnook.”

Biologists have long observed that some sea creatures glow in the dark. In 1962, Dr. Shimomura, then a researcher at Princeton, and Frank Johnson, a Princeton biology professor, isolated a specific glowing protein in the Aequorea victoria, a jellyfish that drifts in the ocean currents off the west coast of North America.

The protein looked greenish under sunlight, yellowish under a light bulb and fluorescent green under ultraviolet light. Dr. Shimomura and Dr. Johnson called it the green protein, but now it is known as green fluorescent protein, or G.F.P. for short.

The green fluorescent protein consists of a chain of 238 amino acids bent into a beer can-like cylindrical shape, and for two and a half decades it remained a little-known biological curiosity.

Dr. Chalfie first heard about the protein at a seminar in 1988, and thought he might be able to use it in his studies of Caenorhabditis elegans, a transparent roundworm.

“It didn’t take much to realize that if I put that fluorescent protein inside this transparent animal, I would be able to see the cells that were making it,” he said. “And that’s what we set out to do.”

He thought that the fluorescent protein could be made to serve as a biological marker by splicing the gene that makes the protein into an organism’s DNA next to a gene switch or another gene.

“That serves as a lantern,” Dr. Chalfie said, and biologists would be able to see when specific genes turn on or off and where different proteins are produced.

He was not able to pursue the idea until Douglas C. Prasher, a scientist then at the Woods Hole Oceanographic Institution in Massachusetts, found the G.F.P. gene and shared it with Dr. Chalfie in 1992. Dr. Chalfie said that within a month his group was able to insert the gene into E. coli bacteria.

In 1994, Dr. Chalfie and his collaborators reported that they had inserted the protein into six cells of the C. elegans worm. When placed under ultraviolet light, those cells shined green, revealing their location.

For many biologists, it was a surprise that inserting the G.F.P. gene was all that needed; many had thought that other jellyfish proteins would be needed to help G.F.P. fold into its light-emitting shape.

Dr. Tsien was thinking along similar lines as Dr. Chalfie, also contacting Dr. Prasher. But for the biology experiment he wanted to conduct, he needed two colors of fluorescent proteins. Dr. Tsien started mutating the G.F.P gene and looking at the resulting proteins. Some, he found, glowed blue instead of green.

“That was the first evidence you could change the color,” Dr. Tsien said.

Other scientists have since expanded the palette, enlisting similar proteins from corals to produce fluorescent reds. The multiple colors allow biologists to track different processes simultaneously. In one experiment, the brain of a mouse was transformed into a kaleidoscope of color by tagging different nerve cells with different fluorescent proteins.

The protein has even entered the world of art. In 2000, Eduardo Kac, an artist, displayed a green glowing rabbit named Alba, which he had commissioned a French laboratory to modify genetically with the G.F.P gene.

Scientists have also made green-glowing pigs and zebra fish, which they hope will aid research on stem cells and cancer.

Copyright 2008 The New York Times Company

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