"The day I was informed of the Nobel Prize I thought they were taking their hair"

Ada Yonath says she felt really happy to see for the first time the structure of the ribosomes. He had been studying the ribosomes for twenty years and many people who did not believe in his work surrounded him. This work of the ribosomes inspired polar bears, whose final result was the 2009 Nobel Prize in Chemistry.

"The day I was informed of the Nobel Prize I thought they were taking their hair"


For thirty years working with ribosomes, is there still something to investigate?

When I started, people asked me why I had to start studying the structure of the ribosomes, why I didn't grab DNA, or messenger RNA… they told me that before I found anything I would die. But I advanced; I wanted to understand the structure of the ribosomes; once understood the structure with precision to know its function.

And yes, there are still many things to investigate. To begin with, we still do not know how all antibiotics work. And it is very important, since half of the antibiotics used in pharmacies and hospitals are antibiotics that affect ribosomes, since they are interrupted. We try to understand their influence on the ribosomes.

Compared to ribosomes, antibiotics are very small elements. On the human scale, it would be like the struggle between David and Goliath. Therefore, to cause damage, the child must avoid or do something similar to the big one. In the ribosomes, antibiotics must interrupt some of the functions necessary for their proper functioning: reading the messenger RNA through the ribosome, advance of protein synthesis, etc.

Give some example...

For example, chloramphenicol occupies the place where the transfer RNA to the ribosome is associated, that is, where the components of proteins, amino acids, and erythromycin are added to the tunnel of the ribosomes. Proteins advance in the central tunnel of the ribosomes as they form and lengthen. Erythromycin is the most effective of the antibiotics that clog the tunnel and is therefore the best. Thus, consumption of 500 mg of another antibiotic four times a day for seven days and 500 mg of erythromycin twice a day for four days. It has been the first time that the structure has explained in science what dose it has taken.

Pathogenic bacteria, however, want to survive, as we want, and develop resistance. They alter their genome to become resistant: they produce proteins that resist antibiotics or alter the "pocket" of the antibiotic (zone of binding of the antibiotic to the ribosome). The bacteria change the atoms of the place where the strongest link is made.

I think the XXI is a resistance. one of the greatest problems of the twentieth century; people can be affected and recovered, while resistances can be eliminated by pneumonia.

Are there significant differences between ribosomes of superior animals and bacteria?

Of course! Ribosomes in humans or mammals are 40% higher than those of bacteria. However, sometimes the same processes are given. In the studies we have seen that the active regions of all ribosomes are practically equal. What has changed is the interaction between ribosomes and cells, which has evolved a lot, since animal cells are more complex.

For example, when drinking alcohol we need the alcohol dehydrogenase protein to metabolize that drink. But you don't have to be continually producing alcohol dehydrogenase, because you don't drink constantly. Therefore, ribosoma regulates when and when it does not produce.

But if you use the ribosome of a horse in a human cell, will it fulfill its function?

Yes. If you give them the messenger [RNA], all ribosomes will fulfill the function of forming the protein. They are totally universal.

On the other hand, among the things we want to know there is another one that I think is very important: we have found a small structure in the complex structure of the ribosome, a nucleus, and we believe that it was formed before living beings emerged.

Is the initial structure of the ribosomes?
(Photo: Juan Carlos Ruiz/Press de Fotos)

Yes, and perhaps also the initial structure of life. We are trying to rebuild this structure.

Let's talk a little about the Nobel Prize, what did the Novel bring you to win?

You will forgive me, but I have a standard answer for that question...! [laughter] [laughter]

Yes, the question is also standard, but we want to know how you lived that moment...

I was really happy when I first saw the structure of the ribosomes. In particular, twenty years after its commissioning. I started on November 15, 1979 and in September 2000 we published the entire first structure.

During that time I faced the criticism of many people. People did not believe in the structure of the ribosomes and I also advanced very slowly. I needed months to create very small ribosome crystals. Then, when we managed to make measurements with these crystals it also took time: the detectors were not good, we did not put the crystals in the proper position, we damaged the samples... But I continued to work.

Then, the day I was informed of the Nobel Prize, I thought they were taking their hair. He had just returned from a congress from San Sebastian to Tel Aviv. They called me at ten in the morning, from New York, saying that the next day they were going to give me the Nobel Prize in Chemistry.

I thought: "In New York they are three in the morning. These are taking my hair." And I answered what he called to me: "All the night of revelry and you are drinking, go to sleep! ". Therefore, it is clear that he was not willing to receive the prize. Yes, when the next day they asked me if I would accept the prize, I certainly said yes.

But was it important for you to receive the Novel?

No. That is, it was not the most important thing. As everyone was laughing on my own, it was a great Novel award. But many people believe we work to win prizes, and many believe their work is worthy of the prize. In my case, however, my goal was to understand.

And for the scientific field? Has the triumph of the Novel influenced, have investigations increased?

I do not know how to answer whether or not he drove the field of the ribosomes; I have seen that yes, he has influenced the young. Children and young people consider the work of scientists as a boring work. I, however, give many lectures to children, and receive letters from children from around the world, from 5-6 to 14-15 years. They ask me for photos, they tell me they want to be like me... One asked me: "Do you present yourself the next year? ". Things like this.

History of the relationship between ribosomes and polar bears
The history of polar bears began at a congress in Canada. At that congress I contacted the researcher Wittman of the Max Planck Institute in Berlin. I was already working with ribosomes and had managed to create very small crystals. When I informed him of them, he proposed to collaborate in a five-year collaboration.
It was in February 1978 and we decided to start the collaboration in May 1979. In February of that year, however, when I was riding, I suffered an accident. I fell from the bike and had contusion in the head. I was very serious in the hospital and spent a lot of time until I formed. Therefore, I could not go to Berlin, were other members of my team.
By the time I recovered quite a lot, an important part of the work was done and was still very weak. The only thing I could do was read. So I read it, read it, and read it. And I read it about polar bears. Here begins the scientific part of the story.
In the study of ribosomes there was a problem: They had been trying to crystallize the ribosomes for 20 years, but they all failed. Several studies concluded that it was impossible to crystallize the ribosomes: they move too much, have a structure too heterogeneous and degrade too quickly. More homogeneous crystallization structures are needed so that all crystals are equal. Until then the trials were performed with ribosomes of the bacterium E. coli, which is extremely sensitive.
Meanwhile, I read about bears. I read in a magazine that the ribosomes during the hibernate are organized in the membranes of the cells, they align. There I saw, on the one hand, that against what was thought, the ribosomes can accumulate ordered. Therefore, it was something that could be done. And on the other hand, I learned that the goal of this organization is to protect the ribosomes so that they do not spoil. After the winter, they begin a phase of great activity, for which they must have ribosomes prepared to form all the necessary proteins.
I thought this mechanism of nature to maintain active ribosomes could be useful for research. However, I wanted to use bacteria, not bears. All we knew at that time about ribosomes was about the ribosomes of bacteria. E. coli.
So I had to start from the active ribosomes. And it was that he did not know anything about the formation of the ribosomes, so he could not know which conformation was good and which was not. Being active ribosomes, I knew they had a good formation.
For having more active ribosomes, I thought of getting ribosomes from bacteria living in difficult conditions. People were surprised because they did not want E. coli, but shocks. I started researching with thermophilic bacteria and halophilic Dead Sea (Bacillus stearothermophilus). I thought that ribosomes of bacteria living in salinity of four molars and at 50 degrees would have more chances of staying active. It was the only way to get active ribosomes, and it remains...
Lakar Iraizoz, Oihane
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