I see interdisciplinarity today as a huge advantage and a necessity, says graduate Janovič

Tomáš Janovič from the National Centre for Biomolecular Research focuses on genome stability and the protection of telomeres, the ends of chromosomes. He has received prestigious grants for his research, including the MSCA Individual Fellowship and GAMU MASH StG/CoG. He is currently looking for PhD students to join his team. “Understanding how a single protein complex can both protect telomeres and allow their elongation could open up new possibilities for targeted cancer treatment,” says Janovič, a graduate of Biomedical Engineering and Bioinformatics.

6 May 2026 Adéla Lerchová

Photo: Mgr. Tomáš Brom, Ph.D.

Ing. Tomáš Janovič, Ph.D.

Tomáš Janovič completed his PhD in telomere biology – the protective ends of chromosomes – at the Faculty of Science. After a three-year stay in the United States, he returned to the Czech Republic last autumn and secured a postdoctoral position through an open call at NCBR.

He is currently pursuing his own research on genome stability and telomere protection, funded by a prestigious MSCA Individual Fellowship, which was ranked as the most successful project submitted under Masaryk University.

 

Your scientific path is relatively unusual. You joined Honeywell after completing your master’s degree in Biomedical Engineering and Bioinformatics (VUT–MUNI), and only later returned to academia for a PhD in Life Sciences. What made you leave the commercial sector and come back to academic research?

Although I had more or less ruled out doing a PhD at first, after less than two years I started to really miss scientific and research work, so I decided to return to academia.

Working in a corporate environment was initially a new and interesting experience, but over time I felt it wasn’t where I wanted to be long-term. That said, I definitely don’t see that period as a negative. On the contrary, it helped me clarify what I truly want to focus on and what actually makes sense to me.

I was also very lucky to have my supervisor, Associate Professor Ctirad Hofr, who was willing to take on someone without a strictly biological or biochemical background and thanks to that, we can have this interview today.

Your research focuses on genome stability – specifically telomere protection. Why are telomeres so crucial for understanding how cells function, and why are they almost universally “hijacked” in cancer?

Telomeres are the ends of our chromosomes. You can think of them like the plastic tips on shoelaces – if they’re not protected, they start to fray. Similarly, chromosomes need protection; otherwise, they become damaged and unstable. That’s exactly the role telomeres play.

At the same time, in most normal cells (unlike stem cells), telomeres gradually shorten with each cell division. In a way, they determine how many times a cell can still divide – they act as a kind of “biological timer” of its lifespan.

Cancer cells, however, have figured out how to bypass this mechanism. Like stem cells, they can extend their telomeres again, which gives them the ability to divide almost indefinitely.

Your research focuses on the shelterin protein complex. How would you describe its role in protecting chromosome ends, and what remains unclear in this area?

Shelterin is a fascinating complex made up of six different proteins. What I find particularly interesting is that it can perform two seemingly contradictory functions at the same time.

On the one hand, it organizes telomeric DNA into a protective loop, shielding chromosome ends from damage or unwanted repair. On the other hand, it allows access to telomerase – the enzyme that extends telomeres – and actively regulates their length.

We still don’t fully understand how a single protein complex can both protect telomeres and enable their elongation. Understanding this delicate balance could open up new possibilities for targeted cancer therapies, where telomere length regulation plays a key role.

During your time at Michigan State University, you studied telomere protection in human cells using advanced imaging methods. What made this experience pivotal for your scientific direction?

Besides learning a range of technically demanding methods, this experience was crucial for another reason. I had the opportunity to work on my own project – one that truly motivated me and helped me build the expertise I now rely on in my independent research.

It also brought me key contacts, new collaborations, and visibility within the scientific community. And that’s absolutely essential. Science can’t be done in isolation, it thrives on sharing ideas and collaboration.

That’s why I see openness and sharing know-how as an important part of my own research as well. We try to support open scientific practices and actively share our experience and methodologies with others.

Do you see having an interdisciplinary background – like your technical foundation – as an advantage, or is it better to specialize narrowly from the start?

Personally, I see interdisciplinarity today as a huge advantage – and to some extent, a necessity. The most interesting discoveries often happen at the boundaries between fields, where different ways of thinking come together.

When you can combine technical, biological, or even physical perspectives on the same problem, you start asking questions that might never occur to you within a single narrow specialization.

That said, it’s a more demanding path. It means mastering one field in depth and then starting again as a beginner in another. That can be frustrating and requires a lot of patience and persistence – qualities that are essential in science anyway.

I don’t think there’s a single “right” path, though. Some people thrive in deep specialization and become world experts in a very specific topic. Others connect fields and build bridges between them. Ideally, these types of people meet in one team – and that’s exactly the kind of team I’d like to build.

You’re currently recruiting PhD students. What can a student in your group expect to work on? Will they get hands-on experience with modern microscopy and data analysis, or start with routine experiments?

Work in our group is really diverse. Students get to work with modern microscopy techniques as well as advanced data analysis which is definitely more than just “clicking through software.”

At the same time, they need to master the fundamentals of molecular biology. Without those, the more sophisticated experiments simply wouldn’t be possible.

A defining feature of our lab is the emphasis on visualization. When we study something, we want to actually see it – capture it in an image or video, ideally in a living cell. Students can, for example, analyze the movement of individual molecules in real time or take part in studying telomeric chromatin structure using advanced imaging techniques.

That said, the specific direction is always tailored to what each student enjoys most. Some get excited about data and quantitative analysis, others about hands-on experimental work or structural biology. I try to support everyone in what motivates them and where their strengths lie.

Another big advantage is the interdisciplinary environment. Students learn from each other, share know-how, and gain a broad overview of current research possibilities.

Your project combines fluorescence microscopy, single-molecule approaches, targeted genome editing, and cryo-electron tomography. What does this interdisciplinary combination allow you to see that wasn’t possible before?

Being able to observe protein behavior at high resolution, in real time, and directly in its natural environment – a living cell – is the dream of almost every cell biologist. We’re not quite there yet, but combining these methods brings us much closer.

Targeted genome editing allows us to study proteins in their natural context, without artificial modifications that might affect their function. Single-molecule imaging then provides detailed insights into dynamics – when a protein binds, how long it stays, and how it moves within the cell.

Cryo-electron tomography, on the other hand, gives us a structural view at very high resolution, revealing what these molecular complexes actually look like.

By combining these approaches, we can link structure with dynamics. We don’t just see what a protein looks like – we see how it behaves, directly in the cell. That’s something traditional methods simply can’t achieve.

You received the prestigious Marie Skłodowska-Curie Action Postdoctoral Fellowship (MSCA PF). What do you think made your project successful?

That’s a tough question. I wasn’t on the evaluation panel. But I think it was a combination of factors.

Many excellent early-career researchers apply with strong scientific questions and well-designed research plans, so often it comes down to small details like the potential for professional growth, the expected impact of the results, or the quality of training.

All parts of the application need to fit together. That’s why it’s crucial not to underestimate any detail and to think through every aspect carefully. Another factor is time. I worked systematically on the proposal for more than half a year in advance.

What advice would you give students at the beginning of their careers who are deciding between interdisciplinary research and, say, trying out a career in industry?

This is very individual, but I’d definitely encourage people not to be afraid of making a bigger change or taking some risks. Often, a new perspective – whether from a different field or environment – can be exactly what pushes a project forward.

 


More articles

All articles

You are running an old browser version. We recommend updating your browser to its latest version.