Thomas A. Steitz
Interview with the 2009 Nobel Laureates in Chemistry Venkatraman Ramakrishnan, Thomas A. Steitz and Ada E. Yonath, 6 December 2009. The interviewer is Adam Smith, Editor-in-Chief of Nobelprize.org.
The 2009 Nobel Laureates met at the Bernadotte Library in Stockholm on 9 December 2009 for the traditional round-table discussion and TV program ‘Nobel Minds’. The Laureates discussed the controversy surrounding President Barack Obama’s Nobel Peace Prize, climate change data and science’s integrity in the face of political policy.
Participants of the 2009 edition of Nobel Minds were the Nobel Laureates in Physics Willard S. Boyle and George E. Smith; the Nobel Laureates in Chemistry Venkatraman Ramakrishnan, Thomas A. Stetz and Ada E. Yonath; the Nobel Laureates in Physiology or Medicine Elizabeth H. Blackburn, Carol W. Greider and Jack W. Szostak; the Laureates in Economic Sciences Elinor Ostrom and Oliver E. Williamson. Program host: Zeinab Badawi.
Telephone interview with Thomas A. Steitz immediately following the announcement of the 2009 Nobel Prize in Chemistry, 7 October 2009. The interviewer is Adam Smith, Editor-in-Chief of Nobelprize.org.
[Thomas Steitz] Hello?
[Adam Smith] Good morning, may I speak to Professor Thomas Steitz please?
[AS] Hello, this is Adam Smith from the official web site of the Nobel Foundation in Stockholm. Congratulations on the award. And, we have a tradition of recording very brief telephone interviews with all new laureates. Would it be possible to record a brief conversation?
[TS] Ah, OK.
[AS] Thank you. So for a starter, I’m right in thinking, I believe, that you and your wife are both biology professors at Yale?
[TS] We’re both professors of molecular biophysics and biochemistry at Yale, yes.
[AS] And when you got the call this morning, were you asleep?
[AS] Nice way to be woken up, I imagine?
[TS] Oh, it is indeed!
[AS] And what for you is the particular joy of trying to unravel these large macromolecular structures?
[TS] Well, I found the most exciting thing about the ribosome was seeing a structure, seeing a large macromolecular assembly that I had no idea what it would look like. And I have to say it was the most exciting time in science that I’ve had, by a lot. Just, you know, it’s like getting to the top of Mt. Everest and seeing the view, it’s terrific.
[AS] There seems to have been this magical year of 2000, when the high resolution structures began to come out.
[TS] That’s correct. Yeah, we… it started coming out in the earlier stages in ‘98 and then of course there’s always communication back and forth about how to do things and it all happened at once after many, many years of not happening. It was great!
[AS] And, it’s all about images, it’s all about building images of the various subunits and putting that together to get a picture of how the ribosome functions. Do you feel that we now have a good picture of the way the ribosome works?
[TS] Oh, I think that it’s an extraordinarily good picture. I mean there’s always more that one can do, of course. And it’s led to insights in a variety of things and most … I think one that will have the most profound effect on the public at large is the ability to use this structural information to design new antibiotics that are effective against disease resistant strains.
[AS] Indeed, you founded a company, Rib-X Pharmaceutical, to pursue that. And it sounds, from what you’re saying, that you’re very hopeful that there will be new classes of antibiotics that result from this?
[TS] Yes, they have one that’s completed Phase II clinical trial successfully and is now ready for Phase III. And they have several others that are coming along in earlier stages, so it’s a rich environment for designing antibiotics and it’s the major target of antibiotics in general anyhow, so … And the structure has been very, very illuminating. Now that wasn’t our original goal in solving the structure. I wanted to understand how it worked! But this was sort of a little, side benefit of learning the structure. This is why I think basic research is very important because it can have applied consequences that you didn’t even think about.
[AS] And it’s an enormously important problem because antibiotic resistance is increasing at a very alarming rate, yes.
[TS] And there was an article in the New York Times about a year ago, two years ago, that said that there were twenty thousand people a year who died of MRSA infections in US hospitals alone. That’s a lot of people.
[AS] One of the things that you contributed was the solution of the phase problem for the larger subunit of the ribosome, which reminds one of Max Perutz who had solved the phase problem for smaller proteins in the 1950s.
[TS] Yes, my idol.
[AS] Because you were a post doc at the LMB in Cambridge for a while?
[TS] I was indeed.
[AS] So, did you encounter him there?
[TS] Oh yes. I knew Max Perutz very, very well. Actually it was Max Perutz who inspired me to go into structural biology when he gave a lecture at Harvard in 1963. As soon as I heard him talk, I decided that this is what I want to do.
[AS] That’s nice to be able to pinpoint it to a single moment.
[AS] Well, thank you very much indeed. I’d just like to finish by asking; would you describe yourself and Ada Yonath and Venki Ramakrishnan as being collaborators or are you friendly competitors?
[TS] Ah, well, we’re not collaborators in the sense that we’ve all worked completely independently. And I’ve known Venki Ramakrishnan much better because he was a post doc at Yale in the ‘80s and so I knew him them and I’ve known him subsequently. So we’ve interacted much more than I have with Ada Yonath.
[AS] OK, thank you. OK, well, I better leave you to get on with this day. Do you know what’s going to happen next?
[TS] Ah, no.
[AS] Well, I leave you to discover.
[AS] And when you come to Stockholm in December to receive the award we have a chance to speak at greater length.
[TS] OK, good.
[AS] OK, thank you and congratulations again.
[TS] Thank you.
[AS] Thank you, bye, bye,
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