The article has recently won the Count István Tisza Foundation for the University of Debrecen Award and the University of Debrecen Publication Award.
"Winning this award is a great honor for me and my team. This is the greatest recognition of my career and scientific work to date," said László Imre, research fellow at the Institute of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, on receiving the Count István Tisza Foundation for the University of Debrecen Award and the University of Debrecen Publication Award.
The scientific article published in Nature Communications summarizes approximately ten years of work, most of which consists of the results of experiments and measurements carried out at the Institute of Biophysics and Cell Biology, University of Debrecen, with the collaboration of Hungarian and foreign partners. The paper has a total of twenty-five authors. The aim of their research was to study a histone variant protein, H2A.Z.
The choice of topic was justified by the outstanding importance of the H2A.Z histone variant, as it is involved in the regulation of fundamental cell functions such as gene transcription, DNA repair, and DNA replication (replication). In other words, it plays a central role in cell function. H2A.Z plays an important role in the development of many tumors, so it also has clinical significance, according to the researcher from the University of Debrecen.
The researchers examined the stability of nucleosomes containing this histone variant. Nucleosomes are part of the chromatin (chromatin = DNA and associated proteins) in the cell nucleus and are the basic units of DNA packaging in the nucleus. Nucleosome stability refers to how strongly the proteins that make up the nucleosome bind to each other and to the DNA wrapped around them. The study examined how DNA is packaged in cells and how this "packaging" can be influenced by a special protein called H2A.Z.
- H2A.Z has a very short, tail-like section at the carboxy-terminal end (consisting of 9 amino acids) which plays a key role in how tightly DNA is wound around nucleosomes and how compact the chromatin structure is. If we remove or block this part with a peptide that we have produced, the chromatin loosens, the genes become more accessible, and the structure of the entire cell nucleus changes. In simple terms, this means that this short protein segment acts like a "switch": when it is "switched on," DNA is tightly packed in chromatin and less accessible; when it is "turned off," the chromatin becomes looser, the DNA becomes more accessible, and the genes can become more active, emphasized László Imre.
This is important because it provides a new perspective on how cells regulate the function of their genes, could help develop more effective anti-cancer therapies or treatments for other diseases, and shows that even a very small protein fragment can have a huge impact on cell behavior.
To conduct the studies, the researchers developed a new, unique, automated quantitative imaging cytometry-based measurement method that allows them to determine how "tightly" DNA is packed in the entire chromatin inventory or selectively in certain regions of it. This measurement can be performed within the cell nucleus, which makes the technique unique.
The research continued after the publication was accepted. In their nucleosome stability studies, the experts analyzed how the spiral twist of DNA (superhelicity) affects the strength of DNA packaging in cells. To do this, they used a special dye (intercalating DNA dye) and high-precision microscopic measurements (FCS). Their latest findings are currently under review.
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