Thomas A. Steitz, a Yale scientist, was awakened at 5:20 a.m. by a call from a man with a Swedish accent.
The man said he represented the Nobel chemistry committee, and informed Steitz that he had won.
Steitz asked to the man to pass the phone around, to make sure the call was not a prank.
“I know some of those people,” said Steitz, who is Sterling professor of molecular biophysics and biochemistry and professor of chemistry at Yale.
It turned out there was no prank call — Steitz had won the 2009 Nobel Prize for chemistry for basic research into how cells make proteins. He will share the $1.4 million in Nobel money with two other scientists.
Steitz, who came to Yale in 1970, determined the molecular structure of the large part of a ribosome, the two-molecule protein in cells that builds other proteins and enzymes, from stomach acid to neurons.
The ribosome consists of two subunits, a large one and a smaller part. The two units are made out of RNA and other proteins.
Proteins are formed when DNA ‘unzips” and a gene is translated into messenger RNA. The strip of mRNA then passes through the ribosome, and transfer RNA attaches amino acids in the proper order to make a protein.
Steitz and colleagues determined the structure of the large — or 50‑s unit — by bombarding protein-RNA crystals with x‑rays.
X‑rays bounce off the atoms leaving a telltale refraction pattern. By analyzing the pattern, Steitz and fellow scientists were able to construct a three-dimensional model of the unit, which contains about 100,000 atoms.
“It’s a very important assembly in the cell. Almost all proteins in the cell are made by ribosomes,” Steitz said.
Steitz began research into the ribosome in 1995, using x‑ray sources at Brookhaven National Laboratory on Long Island and at Argonne National Laboratory outside of Chicago.
The last Nobel prize won by a Yale scientist was awarded in 1989 to Sidney Altman, who discovered a catalytic version of RNA, that he termed the ribozyme. The ribozyme helps to explain how an early “RNA world” evolved into the “DNA world” of the last few billion years.
Steitz said that detailed knowledge of the ribosome should allow researchers to develop novel antibiotics.
Ribosomes are highly conserved, meaning that the structure does not change very much over long periods. Biologists could develop molecules that jam up the ribosome of bacteria otherwise resistant to current antibiotics.
Bacteria, such as Streptoccocus can mutate rapidly, leaving some pathogens invulnerable to penicillin, and other types of antibiotics. However, ribosomes are not likely to mutate.
Steitz and colleagues founded a New Haven biotechnology company, Rib‑X in 2000 to develop new antibiotics. Rib‑X has two potential infection-fighting molecules in phase 2 clinical trials and three more under development.
Steitz said he plans to “keep doing what I’ve enjoyed doing all along, working in the lab and working in the garden.”
Steitz said he has not considered what he will do with his share of Nobel loot, and that no one has yet asked him for a loan.
Steitz is sharing the 2009 Nobel prize for chemistry with Venkatraman Ramakrishnan of the MRC Laboratory of Molecular Biology in Cambridge, England, and Ada E. Yonath, of the Weizmann Institute of Science in Rehovot, Israel.
All three winners produced models of ribosomes, or of antibiotics attached to ribosomes. The prize money will be split in thirds.
Steitz was born in 1940 in Milwaukee and received his bachelor’s degree from Lawrence College in 1962. He was awarded a doctoral degree in molecular biology and biochemistry in 1966 from Harvard. Steitz worked at the MRC Laboratory from 1967 until he joined the Yale faculty in 1970.