WASHINGTON, Oct. 7 (Xinhua) -- Yale University hailed Wednesday the achievements of Professor Thomas Steitz, who was awarded the Nobel Prize in chemistry with two other scientists for creating detailed blueprints of the protein-making machinery within cells, research that's being used to develop new antibiotics.
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."
However, Steitz saw the Prize as a great recognition to both him and his research team.
"A great number of people work together (in my team). Each makes extraordinary important contribution. I'm very grateful for them," Steitz told Xinhua in a telephone interview.
The professor felt "very excited" while getting a call from Stockholm, where the Nobel jury announced this year's Nobel Prize winners. "It is always a pleasure to be appreciated. Everybody feels that way."
Steitz said it's a surprise for him to get the prize. "A number of people suggest that is going to happen. But the question is you never know whether or when that's going to happen. Maybe it should happen, it might happen, but that doesn't mean it does happen. So it's always a surprise."
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.
"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 at Yale.
"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."
Steitz told Xinhua he will continue to work on ribosome. Several colleagues in Yale and he have established 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 functionof the ribosome and has yielded several distinctive new antibiotics that can be used for the treatment of multi-antiobiotic resistant infections."
Steitz is also a Howard Hughes Medical Institute (HHMI) investigator. The HHMI got two Nobel Prizes this week. Jack Szostak, another HHMI researcher was awarded Monday the Nobel Prize in Physiology or Medicine for discovery of how chromosomes are protected by telomeres and the enzyme telomerase.
"It's fantastic news. I don't think that ever happens before," Robert Tjian, president of HHMI, told Xinhua through telephone.
According to Tjian, there are about 15 Nobel Prize winners that have been working for the HHMI.
