Author: Alexander Naneyshvili

We once again received wonderful Nobel news today. We were delighted to learn that three long-time NIGMS grantees–Venkatraman Ramakrishnan, Thomas Steitz and Ada Yonath–will share the 2009 Nobel Prize in chemistry  for their “studies of the structure and function of the ribosome.”

Remarkably, at the same 1987 “Evolution of Catalytic Function” Cold Spring Harbor meeting where I first met Carol Greider, I heard Ada Yonath describe her initial attempts to crystallize and determine the structure of the ribosome. Tom Steitz also spoke about his exciting structure determination of DNA polymerase I, and Peter Moore talked about his work on the ribosome using specific deuterium labeling and neutron scattering methods developed in part with Venki Ramakrishnan. The meeting was filled with the promise that we would one day visualize and begin to understand this elaborate RNA-protein machine in atomic detail. More than a decade later, that promise was realized, as recognized by today’s announcement.

The Nobel committee has the daunting challenge of limiting itself to up to three laureates for each prize. Several other long-time NIGMS grantees who also contributed greatly to our understanding of the structure and function of the ribosome include Peter Moore, Harry Noller and Joachim Frank.

We were all very sad to learn of the death of Ruth Kirschstein, M.D., last evening. She will be deeply missed here at NIGMS, NIH, and beyond.

Dr. Kirschstein was an iconic figure at NIH and in the scientific community. She was the long-time director of NIGMS, serving from 1974 to 1993, and was the first female director of an NIH institute. She also served as acting director of NIH, deputy director of NIH, and in other key positions.

Dr. Kirschstein truly represented the best of NIH—public service, wisdom, and deep knowledge and analysis of important problems. She was so profoundly modest that Congress had to surprise her when they acknowledged her contributions and commitment to research training with the naming of the Ruth L. Kirschstein National Research Service Awards.

I am sure much more will be said and written about her in the future, and we will share this with you in the comments section. I encourage you to post your own thoughts about her as well.

We were delighted to learn this morning that long-time NIGMS grantees Elizabeth Blackburn, Carol Greider and Jack Szostak will share the 2009 Nobel Prize in physiology or medicine   for their “discovery of how chromosomes are protected by telomeres and the enzyme telomerase.”

I remember very well the presentation by then-graduate student Carol Greider at the 1987 Cold Spring Harbor Symposium on Quantitative Biology about her purification and initial characterization of telomerase and component RNA. Her passion and enthusiasm for science stood out, even in that high-powered crowd. I also enjoyed working with her when we were colleagues at Johns Hopkins before I came to NIGMS.

The work of Blackburn, Greider and Szostak represents an archetype of curiosity-driven basic research. The fact that DNA synthesis requires a template creates a clear challenge to copying the ends of DNA. The reality of this challenge was clear from Szostak’s studies with linear DNA molecules in yeast. Using a model organism (Tetrahymena) selected for its unusually high abundance of DNA ends, Blackburn’s lab identified telomere sequences and showed, with Szostak, that these sequences did, in fact, stabilize linear DNA molecules in yeast. Blackburn and Greider then set out to detect and purify the enzyme that adds telomeres to DNA.

After their success, they and many other researchers have explored the implications of these observations as they relate to cancer, cellular aging and stem cells. In the years to come, we can expect to see additional implications and broad exploitation of these observations.