CEICS, Campus of International excellence southern catalonia Coordinated by URV · Rovira i Virgili University

Biography

Dr. Ada E. Yonath was born in Jerusalem in 1939 to a poor family. Her memories from her childhood centre on her father’s medical condition and her constant desire to understand the principles of nature. The hard conditions of her young life did not dampen her enormous curiosity. When she was 11 her father died and she began helping her mother in a wide variety of tasks. A year later her mother moved the family to Tel Aviv and it was there that Dr. Yonath completed her high school education.

After finishing her compulsory army service in the Medical Forces, she enrolled at the Hebrew University of Jerusalem where she earned an M.Sc in Chemistry, Biochemistry and Biophysics. She went on to carry out her doctoral studies at the Weizmann Institute, where she attempted to reveal the high-resolution structure of collagen. She continued working on fibrous proteins (muscle) in her first postdoctoral year at the Mellon Institute in Pittsburgh, Pennsylvania and then moved on to the Massachusetts Institute of Technology (MIT) to study the structure of a globular protein staphylococcus nuclease. After completing her postdoctoral research in 1970, she returned to the Weizmann Institute. There, she initiated and established the first biological crystallography laboratory in Israel, which for almost a decade was the only laboratory for such studies. Then, from 1979 to 1984, she was a group leader with Heinz-Günter Wittmann at the Max Planck Institute for Molecular Genetics in Berlin. She was a visiting professor at the University of Chicago from 1977 to 1978, and she headed a Max-Planck Institute Research Unit at DESY in Hamburg, Germany (1986–2004) while conducting her research activities at the Weizmann Institute.

She is best known for her pioneering work on the structure of the ribosome. She is the current director of the Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly of the Weizmann Institute of Science. In 2009, she received the Nobel Prize in Chemistry, becoming the first Israeli woman to win the Nobel Prize out of ten Israeli Nobel laureates, the first woman from the Middle East to win a Nobel prize in the sciences, and the first woman in 45 years to win the Nobel Prize for Chemistry. However, she said herself that there was nothing special about a woman winning the Prize.

Her research

Dr. Yonath focuses on the mechanisms underlying protein biosynthesis by means of ribosomal crystallography, a research line she pioneered over twenty years ago despite considerable scepticism from the international scientific community. Ribosomes translate RNA into protein and because they have slightly different structures in microbes, when compared to eukaryotes such as human cells, they are often a target for antibiotics. She determined the complete high-resolution structures of both ribosomal subunits and discovered within the otherwise asymmetric ribosome, the universal symmetrical region that provides the framework for and navigates the process of polypeptide polymerisation. Consequently, she showed that the ribosome is a ribozyme that places its substrates in stereochemistry suitable for peptide bond formation and for substrate-mediated catalysis. Two decades ago she visualised the path taken by nascent proteins, namely the ribosomal tunnel, and recently revealed the dynamic elements enabling its involvement in elongation arrest, gating, intra-cellular regulation and nascent chain trafficking into their folding space.

Additionally, Yonath described the modes of action of over twenty different antibiotics targeting the ribosome, illustrated the mechanisms of drug resistance and synergism, deciphered the structural basis for antibiotic selectivity and showed its essential clinical usefulness and therapeutic effectiveness, thus paving the way for structure-based drug design.

To enable ribosomal crystallography, Yonath introduced a novel technique called cryo bio-crystallography, which has become routine in structural biology and has allowed intricate projects to be undertaken that would otherwise have been considered virtually impossible.