November 2009

Two ASBMB Members Receive Nobel Prizes

 

Greider

Carol Greider

Steitz

Thomas Steitz

The American Society for Biochemistry and Molecular Biology received a double dose of excitement last month when not one, but two of its members were honored with Nobel Prizes. The good news began with the announcement that Carol Greider, a professor in the department of molecular biology and genetics at the Johns Hopkins University School of Medicine, received one-third of the 2009 Nobel Prize in physiology or medicine, becoming one of 10 women to have won a Nobel in the category (and one of 40 overall). Just two days later, ASBMB member Thomas Steitz, the Sterling professor of molecular biophysics and biochemistry, a professor of chemistry and a Howard Hughes Medical Institute investigator at Yale University, also received a call from Stockholm informing him that he had been awarded one-third of the 2009 Nobel Prize in chemistry.

Greider, who shared the award with her Ph.D. adviser Elizabeth H. Blackburn (currently a professor at the University of California, San Francisco) and Harvard University professor Jack W. Szostak, was awarded the Nobel for her groundbreaking discovery — on Christmas Day — of telomerase, the enzyme that preserves the ends of chromosomes (telomeres) during replication cycles. Over the years, Greider’s continued work in characterizing telomeres and telomerase has further highlighted the importance of this RNA- and protein-containing enzyme complex in maintaining genetic stability. Today, telomerase has become a hot therapeutic target for cancer, aging and other genetic disorders.

Steitz and his chemistry co-recipients, Venkatraman Ramakrishnan of the Medical Research Council Laboratory of Molecular Biology and Ada E. Yonath of the Weizmann Institute of Science, received the honor for their pioneering studies on a key cellular component and therapeutic drug target: the ribosome. The three scientists did what many thought was unfeasible, solving the three-dimensional structure of the organelle (which, like telomerase, contains both RNA and protein components) responsible for translating mRNA templates into functioning proteins. As the ribosome is a primary target for antibiotics, the elucidation of its structure has been instrumental in developing new drugs to combat the ever-growing strains of resistant bacteria.

ASBMB President Gregory A. Petsko was thrilled at the news, and not just because the committee honored outstanding fundamental research driven by pure scientific curiosity. “I can’t think of a prize in recent years that has delighted me more [than the 2009 physiology or medicine],” he said. “Two women, one of whom was the student of the other when the key work was done: This one sends all the right messages.”

A structural biologist himself, Petsko said he also was extremely pleased with the chemistry announcement: “It’s wonderful that the Nobel Committee honored the structure determination of the ribosome. As a window into one of the most important processes in all living cells, this atomic-resolution picture of the machinery that carries out that process is both fascinating and of surpassing beauty.”

With the addition of Steitz and Greider, ASBMB now includes 97 Nobel laureates among current and former members.

Nick Zagorski is a science writer at ASBMB. He can be reached at nzagorski@asbmb.org.

 


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