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Shedding light on luminescence: Scientists visualize structure of the photoprotein aequorin

Anyone who's spent time at a beach on a warm summer night has seen them: luminescing ctenophores that twinkle like tiny stars in moonlit waters. No one knows exactly why these comb jellies flicker and glow, but Marine Biological Laboratory (Cape Cod, Massachusetts) senior scientist Osamu Shimomura now knows a lot more about the structure of the remarkable protein that is not only responsible for this phenomenon, but has proved to be an invaluable tool for researchers studying the role of calcium in disease.

In this week's issue of the journal Nature, Shimomura and his colleagues James Head from Boston University, Katsunori Teranishi from Mei University (Japan), and Satoshi Inouye from Chisso Corporation (Japan), describe the three-dimensional crystal structure of aequorin, the photoprotein that illuminates jellyfish, ctenophores and many other luminescing organisms. The study was supported by the National Science Foundation.

"The work of these investigators has clearly demonstrated how insights into the structure of a protein lead to insights into its biological function...with great potential for molecular modeling and designing new sensors for monitoring other ions in a cell," according to Ralph Addison, program director in NSF's biophysics program, which supported this work.

Since his discovery of aequorin 38 years ago, Shimomura's life's work has been devoted to shedding light on luminescence-a complex chemical reaction within an organism's cells that results in the release of energy in the form of light instead of heat. Shimomura determined years ago that aequorin glows blue when tiny amounts of calcium bind to it.

This discovery led to the use of aequorin as an important biomedical tool for tracking the movement of calcium within cells. Calcium plays a crucial role in the regulation of a variety of biological processes including fertilization, muscle contraction, and the transmission of nerve impulses. Clinicians also recognize tha
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Contact: Cheryl Dybas
cdybas@nsf.gov
703-306-1070
National Science Foundation
17-May-2000


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