Yale’s Thomas Steitz Shares 2009 Nobel Prize in Chemistry — Described Structure and Function of Life’s Protein-Making Factory

Published: October 7, 2009

Thomas Steitz

New Haven, Conn. — Thomas A. Steitz, Sterling professor of Molecular Biophysics and Biochemistry and Professor of Chemistry at Yale University, is one of three winners of the 2009 Nobel Prize in Chemistry for his work describing the structure and function of the ribosome, the protein making factory key to the function of all life, the Royal Swedish Academy of Sciences announced today.

Quotes from October 7:
Quotes by and about Yale’s Nobel Prize Winner Thomas Steitz

Audio from Press Conference:
Nobel Prize Winner Thomas Steitz and President Richard C. Levin

Steitz, a Howard Hughes Medical Institute investigator, shares the $1.4 million award with Venkatraman Ramakrishnan of the MRC Laboratory of Molecular Biology, Cambridge, United Kingdom and Ada E. Yonath, Weizmann Institute of Science, Rehovot, Israel. All three used a technology called X-ray crystallography to map the position for each and every one of the hundreds of thousands of atoms that make up the ribosome. While the work began as a quest to answer basic questions about the makeup of ribosomes, knowledge of its structure has created targets for a new generation of antibiotics.

“Tom Steitz’s relentless pursuit to solve a puzzle at the very foundation of biology inspires us, not only by its intellectual rigor, but also by its potential for the treatment of infectious diseases,” said Yale President Richard C. Levin. “His work is a compelling example of how a quest to answer fundamental questions about life processes can lead to dramatic benefits for mankind.”

The instruction manual for the creation of proteins is DNA, but the ribosome is the machine that translates the encoded information to turn it into proteins. Steitz's work has elucidated the structure and function of the ribosome, an enormously complex ensemble of numerous protein and RNA components.

Steitz and colleagues built upon research of the past half century to describe in minute detail the architecture of the protein-making machinery. Scientific interest on the ribosome has focused on two major subunits. The smaller 30S subunit binds to messenger RNA that harbors the blueprint for protein synthesis. The second subunit 50S carries out the protein synthesis reaction by adding specific amino acid residues onto a growing protein backbone.

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“Steitz’s contributions represent a great leap forward in our quest to understand life,” said Patrick Sung, chairman of the department of Molecular Biophysics & Biochemistry and professor of Therapeutic Radiology. “Moreover, the knowledge garnered from Steitz’s seminal work can be put to practical use. Since bacteria cannot survive without a functional ribosome, Steitz’s studies will likely lead to more efficacious treatment of bacterial infections via the design of new antibiotics that target the ribosome.”

In X-ray crystallography, beams of X-ray pass through and bounce off atoms in protein-RNA crystals. This leaves a diffraction pattern scientists use to discern the three-dimensional atomic details of the molecules under study.

Steitz used a 2.5 billion electron volt x-ray beam at the Brookhaven National Laboratory’s National Synchrotron Light Source and additional data from the Advanced Photon Source at Argonne National Laboratory to study the atomic structure of the 50S subunit.

By 2000, the high resolution enabled the team to resolve the atomic structure of all 100,000 atoms that are well ordered in the crystal.

"I think we were amazed at each stage at the overwhelming complexity of the RNA folding in the ribosome," Steitz said at the time. "But I think the most surprising observation was that the proteins were embedded among the RNA helices, penetrating into the interior of the ribosome like tentacles."

His close collaboration with Yale faculty colleague Peter Moore, Sterling Professor of Chemistry and Professor of Molecular Biophysics and Biochemistry and interactions with William Jorgensen, Sterling Professor of Chemistry, led to the establishment of a company, Rib-X Pharmaceutical, Inc., which is using this knowledge of the structures of the large ribosomal subunit and its antibiotic complexes to create new classes of antibiotics.

“We are extremely happy for Tom on receiving this very prestigious award,” commented Susan Froshauer, CEO of Rib-X Pharmaceuticals. “Rib-X was built on his extraordinary science, utilizes his award winning knowledge of the structure and function of the ribosome and has yielded several distinctive new antibiotics that can be used for the treatment of multi-antiobiotic resistant infections.”

“When these researchers started their work, determining the structure and mechanism of the ribosome seemed nearly impossible,” said Jeremy M. Berg, director of the National Institute of General Medical Sciences. “Their achievement shows how basic research to answer fundamental questions about biology also lays the foundation for medical advances.”

In 2007, Steitz was one of four recipients of the Gairdner International Awards, joining his wife, Joan Steitz, Sterling Professor of Molecular Biophysics and Biochemistry as a recipient of the prestigious award.

Dr. Thomas Pollard, Sterling Professor and Chair of Molecular, Cellular and Developmental Biology; and Dr. Arthur Horwich, the Higgins Professor of Genetics and Pediatrics are also Yale recipients of the Gairdner award. Many scientists have received the award before winning a Nobel Prize.

Steitz was born in 1940 in Milwaukee and received his bachelor’s of arts degree from Lawrence College in 1962 and adoctoral degree in molecular biology and biochemistry in 1966 from Harvard University. He was a postdoctoral fellow at Harvard in1966-67 and at the MRC Laboratory of Molecular Biology, Cambridge, England from 1967-70. He joined Yale as a faculty member in 1970.

*Other awards given to Steitz:
Lawrence University Lucia R. Briggs Distinguished Achievement Award, 2002; Frank H. Westheimer Medal, Harvard University, 2004; Keio Medical Science Prize, 2006; and George E. Palade Award, 2008.

PRESS CONTACT: Bill Hathaway 203-432-1322, Karen N. Peart 203-432-1326