Chemistry Nobel goes to ribosomes, the protein manufacturer

Ribosomes are the manufacturing machines for proteins, which participate in almost every chemical reaction key to life. To study the chemistry of life, it is essential to know the functions and structure of the ribosome. The Nobel Prize in Chemistry goes to three researchers who mapped the positions of atoms in ribosomes, which could lead to more efficient antibiotics.

The 2009 Nobel Prize in Chemistry has been awarded to Venkatraman Ramakrishnan, Thomas A. Steitz, and Ada E. Yonath for enlightening the science community on the structure and function of the ribosome, the protein factory of all living organisms. Out of the three big molecules for life (DNA, RNA, and proteins), proteins arguably do most of the work. They provide structural stability to our cells, give us mechanical motion in our muscles, transport the oxygen that we inhale, and play many other key parts in nearly every chemical reaction that occurs in cells.

DNA contains genetic information, but it is essentially a passive set of instructions and designs that cannot accomplish anything on its own. For there to be life, proteins must help transcribe the data in DNA into RNA, another carrier of information that is more chemically active than DNA, but still less functional than proteins. The messages in the RNA are translated in the ribosome to make specific sequences of proteins, which then goes on to perform essential biochemical functions. Thus, in studying the chemistry of life, we must understand how proteins are made in ribosomes.

The three Nobel winners used X-ray crystallography to identify and map the positions of the atoms in the ribosome to give scientists 3D models to examine and dissect for crucial information on the molecular level. This was an impressive feat as there are hundreds of thousands of atoms involved. Their work has benefited many other areas of research, including the study of antibiotics. As making proteins is essential for bacteria survival, the ribosome is a practical target for drugs. Ramakrishnan, Steitz, and Yonath have provided vital information for the design of new antibiotics.

Venkatraman Ramakrishnan obtained his PhD in physics at Ohio University and studied biology at the University of California-San Diego. He is currently a senior research fellow at the MRC Laboratory of Molecular Biology in Trinity College, Cambridge. Among his first contributions to the study of ribosomes, he published a paper in 1981 and two in 1984 on the structure of a subunit of in an E. coli ribosome. From then on, he continued to solve the structures of the many components in the ribosome, and his latest major work was published in Science last year, providing insight on how protein synthesis knows when to end and detach the finished protein.

Thomas Steitz studied at Harvard and graduated with a PhD in 1966. Since then, he has contributed structural studies on a wide range of proteins, from yeast hexokinase to the HIV reverse transcriptase. Notably, he was the first to provide a structure for DNA polymerase, an enzyme involved in replicating DNA. He has also determined the structure of the 50S subunit of a ribosome along with how it interacts with around two dozen antibiotics. Currently, as a professor of Molecular Biophysics and Biochemistry at Yale University, he is directing his research group in capturing structures of the 70S ribosome in its various states.

Ada Yonath, the first Israeli woman and fourth woman overall to win a Nobel Prize in Chemistry, earned her PhD in X-ray crystallography at the Weizmann Institute of Science, where she is now a professor. She published her first crystal structure in 1965 on a sequence of amino acids, the components of proteins. Over the last 44 years, she has steadily published papers on structures of proteins, RNA related to protein synthesis, and subunits of the ribosome, including seven so far this year.

There is no doubt that Ramakrishnan, Steitz, and Yonath are key figures in the continuing work on discovering the function and structure of the ribosome. Their work has influenced every facet of chemistry, from organic synthesis to biophysical research. Of course, their achievements are built on the work of many others, such as Harry Noller at the University of California-Santa Cruz and Peter Moore at Yale University. Noller and Moore have made significant contributions to deciphering the interactions and activities of the ribosome.