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Nobel Laureate Prof. Ada E Yonath<br />

shared the world’s most coveted<br />

prize in chemistry with Dr Thomas Steitz<br />

and Prof. Venkataraman Ramakrishnan<br />

in 2009. Her pioneering work on<br />

ribosomal crystallography helped in the<br />

precise identification of the structure<br />

and functions of ribosomes and it<br />

opened up immense possibilities of<br />

targeting ribosomes for developing<br />

new antibiotics. The first Israeli woman<br />

to win a Nobel Prize, Prof Yonath<br />

accepted her postdoctoral positions<br />

at Carnegie Mellon University in 1969<br />

and MIT in 1970. She was also group<br />

leader with Heinz-Gunter Wittmann at<br />

the Max-Planck Institute for Molecular<br />

Genetics in Berlin. She was the visiting<br />

professor at the University of Chicago<br />

in 1977-78 and then headed one of the<br />

Max-Planck Institute’s research unit at<br />

DESY in Hamburg, Germany in parallel to<br />

her research activities at the Weizmann<br />

Institute.<br />

Yonath focuses on the mechanisms<br />

underlying protein biosynthesis by<br />

ribosomal crystallography, a research<br />

line she pioneered over twenty years<br />

ago despite considerable skepticism on<br />

the part of the international scientific<br />

community. Ribosomes translate RNA<br />

into protein, and because they have<br />

PROF ADA E YONATH<br />

slightly different structures in microbes<br />

when compared to eukaryotes such<br />

as human cells, they are often a target<br />

for antibiotics. In 2000 and 2001, she<br />

determined the complete high-resolution<br />

structures of both ribosomal subunits<br />

and discovered within the otherwise<br />

asymmetric ribosome, the universal<br />

symmetrical region that provides<br />

the framework and navigates the<br />

process of polypeptide polymerisation.<br />

Consequently, she showed that the<br />

ribosome is a ribozyme that places<br />

its substrates in stereochemistry<br />

suitable for peptide bond formation<br />

and for substrate-mediated catalysis.<br />

In 1993, she visualised the path taken<br />

by the nascent proteins, namely the<br />

ribosomal tunnel, and recently revealed<br />

the dynamic elements enabling its<br />

involvement in elongation arrest, gating,<br />

intra-cellular regulation and nascent<br />

chain trafficking into their folding space.<br />

Additionally, Yonath elucidated the<br />

modes of action of over twenty different<br />

antibiotics targeting the ribosome,<br />

illuminated mechanisms of drug<br />

resistance and synergism, deciphered<br />

the structural basis for antibiotic<br />

selectivity and showed how it plays a key<br />

role in clinical usefulness and therapeutic<br />

effectiveness, thus paving the way for<br />

structure-based drug design.<br />

For enabling ribosomal crystallography,<br />

Yonath introduced a novel technique—<br />

cryo bio-crystallography, which became<br />

routine in structural biology and allowed<br />

intricate projects otherwise considered<br />

formidable.<br />

At the Weizmann Institute, Yonath<br />

is the incumbent of the Martin S. and<br />

Helen Kimmel Professorial Chair. She<br />

is also a member of the United States<br />

National Academy of Sciences, the<br />

American Academy of Arts and Sciences,<br />

the Israel Academy of Sciences and<br />

Humanities, the European Molecular<br />

Organisation and the European Academy<br />

of Sciences and Art. In 2014, Prof.<br />

Yonath was named a member of the<br />

Pontifical Academy of Sciences by Pope<br />

Francis. Her other awards and honours<br />

include the Israel Prize (2002), Harvey<br />

Prize (2002), Massry Prize (2004),<br />

Paul Karrer Gold Medal (2004), Horvitz<br />

Prize (2005), Wolf Prize in Chemistry<br />

(2006), Rothschild Prize in Life Sciences<br />

(2006), The EMET Prize for Art, Science<br />

and Culture in life sciences (2006), Paul<br />

Ehrlich and Ludwig Darmstaeder Prize<br />

(2007), Albert Einstein World Award of<br />

Science (2008), Wilhelm Exner Medal<br />

(2010) and Honorary Doctorates from<br />

several universities.<br />

within the living organisms as a process of getting adapted to<br />

their living environment and there is constant fight that takes<br />

place between one and the other for survival.<br />

Do you think Indian scientists could have achieved more<br />

had the government been more supportive and encouraging<br />

in research and development here?<br />

I don’t know about the support system in India. So, I<br />

can’t comment on that. But I can say that Indian scientists<br />

have been doing well in many areas. There is good science<br />

done in India, which may not be in antibiotics or new drug<br />

development. But it is cleverer in many other areas. Also, there<br />

are good Indian scientists outside the country who are brilliant<br />

and much more capable than others.<br />

The problem that I really see now everywhere is a lack<br />

of support for basic science. Original discoveries should<br />

be encouraged by governments and other systems. Basic<br />

science that tries to understand what is not<br />

understood so far brings real changes in<br />

the society and that should be the focus of<br />

research.<br />

I know that your best advice to young<br />

and aspiring scientists is not to seek advice.<br />

Could you elaborate on this?<br />

Because everybody has to develop the<br />

way they are. Let the young minds grow with<br />

what he or she is really passionate about. It<br />

is the self-curiosity that leads one to discover<br />

new things and that is the kind of research<br />

that the world is looking for and will help<br />

it progress. Taking advice is like copying<br />

someone else, and it will not work the same<br />

way for the other or result in anything new.<br />

<strong>March</strong> <strong>2019</strong> / FUTURE MEDICINE / 39

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