Q&A with Doctor Sandro Ataide

September, 2012

Sandro Ataide

Dr. Sandro Ataide was appointed Lecturer in the School of Molecular Bioscience in 2012, in the area of Structural Biology with emphasis on X-ray Crystallography. Dr. Ataide received his BSc in Chemistry at UNICAMP (Brazil) in 1999 where he held two Research Fellowships (CNPq in Physical Chemistry and FAPESP in Organic Chemistry), and his MSc in Biochemistry at the University of Sao Paulo (Brazil) in 2001. He was awarded his PhD from the Ohio State University (USA) in 2006 where his work focused on understanding how aminoacyl-tRNA synthetases (aaRS) have evolved to efficiently select their substrates (amino acid and tRNA) in order to provide new insights into the development of inhibitors for these essential enzymes. During his PhD, Dr. Ataide received a Predoctoral Fellowship from the American Heart Association and was awarded a Phi-Kappa-Phi Honours. He started his Postdoctoral work with Professor Jennifer Doudna at UC Berkeley (USA) at the end of 2006 where he started his crystallographer career studying the Signal Recognition Particle (SRP). In 2009 he moved to ETH Zurich (Switzerland) to continue his work with SRP and ribosome under the guidance of Professor Nenad Ban where he was a recipient of the ETH Postdoctoral Fellowship. His research targeted the structural and molecular characterization of RNA molecules in RNA-protein complexes using structural biology methods. In 2012 he was awarded the Selby Research Award for his excellence in research targeting eukaryotic RNA-protein complexes.

Do you remember when the idea first crystallized that you would become an academic?

Yes! I remember I was 5 years old in a swimming pool with my family, and they asked me what I wanted to be when I grew up... Even though at the time I had no idea what I meant, I said I wanted to be a teacher of the teachers! It was only later on when I was in high-school Chemistry that I realised what it meant for me and that I wanted to become an Academic. To this day, my entire family remember that conversation in the swimming pool.

Who do you think has been your most influential mentor(s) during your scientific career?

I think every single person I have worked with has been a mentor in some way, because everyone has something to offer and to teach you. If they're not showing you how to do things a certain way, it can be how not to do something. If I had to pick one particular person, it would be Michael Ibba, my PhD advisor at OSU. I've also learnt a lot from Jennifer Doudna and Nenad Ban - my previous bosses. When I have questions and uncertainties it's still Michael that I contact.

What discovery, related to your research, would you most want to be awarded the Nobel Prize for? That is, what do you think is the most pressing and exciting question in your field?

That's a hard one as there have already been Nobel Laureate winners for the things that I'm working on. I usually work on topics that are very difficult to work with, but I'd like to start working with getting structures of non-coding RNAs - it's upcoming and there's lots to be developed and discovered.

What are the most exciting things happening in your lab at the moment?

The most exciting thing at the moment is just setting up the lab and getting people to come over and work with me on developing my projects on RNPs and non-coding RNAs.

We're currently working on the structure of the eukaryotic Signal Recognitition Particle (SRP), that is a ribonucleoprotein complex formed by one RNA and six proteins which is responsible for recognising and bringing the translating ribosome to the endoplasmic reticulum. It sorts the nascent proteins and is hence a very important complex for cell survival. In 1999 the Nobel Prize was awarded to Dr Günter Blobel - he had the idea that proteins must have certain tags/flags which tells where and how the proteins need to be sorted and correctly delivered to their cellular compartment. Still after so many years, we still haven't seen the complete structure of the complexes and still don't have a precise mechanism of how these work.

What do you enjoy most about being in academia?

I love being able to choose the problems that I want to solve and to ask the questions and then find the answers... then ask more questions and perpetuate the cycle over and over. I love that I have the freedom to choose the path that I want, and being able to use my abilities to find a solution.

What would you do differently in your academic career if you had your time over?

That's a hard question - because some days you wake up and think you would do everything differently (to be faster or bolder)... but other times you think 'No, everything is right', and you're keeping the flow. If I was to do something different I wouldn't be so afraid of losing time, and I would have undertaken more internships at different universities during my undergraduate years. I regret not putting a break on my undergraduate degree to go and spend more time abroad.

What are you most passionate about outside the laboratory?

Most certainly my family and also sports - I love doing triathlons and I like skiing, tennis, and all sorts of sports. I also love cooking. It would be my second career - especially molecular cuisine, as I love the idea of applying science with food. My wife and I went to Heston Blumenthal's latest awardee restaurant Dinner in London the night before he was voted one of the top 10 best restaurants of the year. I find cooking very fascinating - it's like having a laboratory at home in which you eat the result of your experiment!

What achievement outside science are you most proud of?

It's hard because there are so many, it's difficult to choose just one! I guess I could say I'm proud of being able to have kept communication open with my family and friends, and still being knowledgeable about everything that's going on in Brazil even though I left over 10 years ago. I use the network and media to stay informed, and my wife and I Skype with our families at least once a week.