Lawrence University Graduate Awarded Nobel Prize in Chemistry

APPLETON, WIS. — Thomas Steitz, a 1962 graduate of Lawrence University, has been named one of three recipients of the 2009 Nobel Prize in Chemistry the Royal Swedish Academy of Sciences announced today.

Steitz, a Howard Hughes Medical Institute investigator at Yale University, is the first Lawrence graduate ever to win a Nobel Prize.

Thomas Steitz

Steitz, along with Venkatraman Ramakrishnan of the Medical Research Council Laboratory of Molecular Biology and Ada E. Yonath of the Weizmann Institute of Science, were recognized for their research on the structure and function of the ribosome.

In announcing this year’s Nobel Prize winners in chemistry, the Royal Swedish Academy cited the three scientists for their work that shows what the ribosome looks like and how it functions at the atomic level. All three have employed x-ray crystallography, a method that maps the position for each of the hundreds of thousands of atoms that make up the ribosome.

Steitz, who earned a bachelor’s degree in chemistry from Lawrence, uses the methods of x-ray crystallography and molecular biology to establish the structures and mechanisms of the proteins and nucleic acids involved in gene expression, replication, and recombination. In x-ray crystallography, protein crystals are bombarded with intense x-ray beams. As the x-rays pass through and bounce off of atoms in the crystal, they leave a diffraction pattern, which can then be analyzed to determine the three-dimensional shape of the protein.

According to the Howard Hughes Medical Institute Web site, an understanding of the ribosome’s innermost workings is important for a scientific understanding of life. Many of today’s antibiotics cure various diseases by blocking the function of bacterial ribosomes. Without functional ribosomes, bacteria cannot survive. A better understanding of ribosomes is crucial for the development of new antibiotics.

While research on ribosome function has been conducted for 50 years, generating massive amounts of information, no group has succeeded in creating an accurate three-dimensional map until now.

“Our previous maps of the 50S subunit at nine- and five-Ångström resolution gave us some hints at the structure, but not until we achieved the 2.5-Ångström resolution could we resolve the atomic structure of all 100,000 atoms that are well ordered in the crystal,” said Steitz, Sterling Professor of Molecular Biophysics and Biochemistry and Professor of Chemistry at Yale University. “This structure is about four times larger than any other such structure that has ever been determined, and the 3,000 nucleotides of RNA increased the amount of known RNA structure by about 4 to 5 fold.”

According to Steitz, the process of achieving such high resolution meant painstakingly improving the process of growing larger, more complete ribosome crystals, and solving structures of those crystals at progressively higher resolution. Each lower-resolution map provided information that could help the scientists understand the ultimate high-resolution map, he said. The high-resolution structure offered a pathway to far deeper understanding of the protein-assembling machinery.

“We’re certainly not done with the scientific challenges presented by the ribosome,” said Steitz. “Although I must say I do feel as if we’re standing on Mount Everest at the moment and I’m now looking to find K2.”

– excerpted from Howard Hughes Medical Institute Web site

Robert Rosenberg, professor emeritus of chemistry at Lawrence was Steitz’ academic advisor. He remembered him as a student with an unusually high-degree of curiosity.

“He was very inquiring, more so than most students,” said Rosenberg, who said he was “thrilled” at Steitz’ latest recognition.

“I’ve been hoping for this for years,” said Rosenberg, who has remained close to Steitz over the past four decades. “For a while I thought it wouldn’t happen, because they had awarded Nobel Prizes to several x-ray crystallographers over the years and I thought they may have exhausted the list.

The Nobel Prize is the latest in a long list of awards Steitz has received during his distinguished career. Among his many other honors are the Pfizer Prize from the American Chemical Society, the Lewis S. Rosenstiel Award for distinguished work in basic medical sciences, the 2001 Newcomb Cleveland Prize from the American Association for the Advancement of Science, the 2006 Keio Medical Science Prize and the prestigious 2007 Gairdner International Award.

Lawrence awarded Steitz an honorary doctorate of science degree in 1981 and recognized him with its Lucia R. Briggs Distinguished Achievement Award in 2002. Steitz served as the keynote speaker at dedication ceremonies in 2000 of Lawrence’s Science Hall.

After earning his bachelor’s degree at Lawrence, Steitz earned his Ph.D. in molecular biology and biochemistry at Harvard University. He is a member of the National Academy of Sciences and the American Academy of Arts and Sciences. He also has been elected a fellow of the American Association for the Advancement of Science and the American Academy of Microbiology.

Dr. Steitz was the commencement speaker at Lawrence University on June 13, 2010.  That same weekend, Science Hall was renamed the Thomas A Steitz hall of Science.