About us

A Szentágothai János Kutatóközpont a PTE korszerű, nemzetközi tudományszervezési és menedzsment normák szerint kialakított új intézménye, amely az élettudományi, élettelen természettudományi, valamint környezettudományi oktatás...

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Molecular biophysics research group

  • Research concept
  • Members
  • Publications
  • Awarded projects
  • R and D results
  • Services
  • Laboratories, instruments
  • Galleries

The design and development of the Unit was manifested in collaboration with other related research groups in the Szentágothai Research Centre. The most important aim of the Unit is to provide modern, efficient and versatile research environment for the scientists and other corresponding investigators, so that they have excellent facilities for the engineering and preparation of biological samples of various organisation levels. Thanks to the functional multiplicity of the instrumentation available in this Unit, samples of peptides, proteins, cells and tissues can effectively be processed in the laboratory. Modern and powerful systems and applications are available for the extraction and modification, and also for the expression and purification of proteins. Fluorescent protein modifications are also possible. The conditions are provided for the use of numerous commercial preparation kits, and thus the investigation of cells and cell populations can also be manifested in this research environment. If the appropriate corresponding preliminary preparations are provided, the Unit will also provide appropriate conditions for the research with more complex biological systems, such as tissues. Based on these advances and the expected future applications the optimisation of the current set-up of the Unit is constantly in progress.
According to the current strategy the research group carries out investigations in collaboration with other groups and core facilities of the Science Building. As the optimal use of the available infrastructure assumes the application of various biophysical methods, the Bio-Imaging Center and the Spectroscopy Laboratory are considered to be the most important from these facilities.
The studies of the Biophysics Research Group are focused on the description and understanding of cellular processes essential in the function and reproduction of living cells. These processes are tightly connected to the cytoskeleton of these cells. The cytoskeleton is composed of microtubules, intermediate filaments, and actin based microfilaments. From these subsystems our research is dealing with the function and regulation of the microfilament system, and the more than 60 protein families associated to these filaments. The aim of these investigations is to characterise the molecular mechanisms underlying the function of the microfilaments, to understand the corresponding protein-protein interactions, and to describe the related changes I cell morphology.
We aim furthermore to investigate the constituents of the bacterial cytoskeleton at molecular level. Among the several types of the bacterial cytoskeleton we focus on the structure and function of the actin ortholog MreB protein. The cytoskeleton was discovered recently in prokaryotes and seems to be crucial for their survival and reproduction. Therefore, understanding the organization of this skeletal system in detail can provide essential information from an epidemiological point of view as well as can contribute to better coping with the increasing antibiotics resistance of bacteria.

Gábor Hild, Lajos Kalmár, Roland Kardos, Miklós Nyitrai, Beáta Bugyi The other side of the coin: Functional and structural versatility of ADF/cofilins. European Journal of Cell Biology, Volume 93, Issues 5–6, May–June 2014, Pages 238–251
http://www.sciencedirect.com/science/article/pii/S0171933513000964

Kis-Bicskei  N., Vig A., Nyitrai M., Bugyi B., Talián, G. Purification of brain tropomyosin 3 and characterization of its interactions with actin. Cytoskeleton 2013 Nov;70(11):755-65. doi: 10.1002/cm.21143
http://www.ncbi.nlm.nih.gov/pubmed/24124168

Ujfalusi Z.,  Kovács M., Nagy T.N., Barkó Sz., Hild G., Lukács A., Nyitrai M., and Bugyi B. (2012) Myosin and tropomyosin stabilize the conformation of formin-nucleated actin filaments. The Journal of Biological Chemistry, 287, 31894-31904.
http://www.ncbi.nlm.nih.gov/pubmed/22753415

Debertin G, Kántor O, Kovács-Öller T, Balogh L, Szabó-Meleg E, Orbán J, Nyitrai M, Völgyi B. (2015) Tyrosine Hydroxylase Positive Perisomatic Rings are Formed around Various Amacrine Cell Types in the Mammalian Retina. Journal of Neurochemistry, doi: 10.1111/jnc.13144. [Epub ahead of print]
http://www.ncbi.nlm.nih.gov/pubmed/25940543

2013. 01. 01. – 2015. 12. 31. OTKA NN 107776, Unique principles in an ancient biological system: structional and functional properties of bacterial filament proteins. (25.188M HUF)
2013. 11. 01. – 2017. 10. 31. OTKA K109689, Investigating the mechanisms of thin filament assembly during myofibrillogenesis. (23.712 M HUF)
2014. 01. 01. – 2014. 12. 31 Magyary Zoltán Postdoctoral fellowship, A disordered protein in an ordered structure. The role of SALS in sarcomerogenesis.
2011. 04. 01. – 2013. 12. 31. OTKA PD83648, Molecular basis for the actin and tropomyosin isoform specific regulation of the actin cytoskeleton. (27.021 M HUF)
2011. 09. 01. – 2013. 12. 31. Bolyai János Research Fellowship, Molecular basis for the functional polymorphism of the actin cytoskeleton.

http://aok.pte.hu/biofizika

Gabor Hild, Beata Bugyi and Miklos Nyitrai. Conformational Dynamics of Actin: Effectors and Implications for Biological Function. Invited review. 2010. Cytoskeleton, 67(10), 609-29.

Szilvia Barkó, Beáta Bugyi, Marie-France Carlier, Rita Gombos, Tamás Matusek, József Mihály and Miklós Nyitrai. Characterization of the Biochemical Properties and Biological Function of the Formin Homology Domains of Drosophila DAAM. 2010. J. Biol. Chem., 285(17),13154-69.

Instrumentation for the preparation of peptides, proteins, cells and tissues.

Sample preparation and approaches for fluorescence spectroscopy and microscopy invetigations
The Unit performes steady state and time resolved fluorescence spectroscopy measurements for applicants. The applied Jobin Yvon instrument is capable of fluorescence detection not only in the UV and the visible range but also in the infrared region. One can perform time resovelved fluorescence experiments with couple of hundred picosecond resolution (depends on the applied wavelength). We can provide for the external users help and assistance with their experiments, choosing their fluorophores or the experimental method for example.

Besides spectroscopic investigations the Unit provides confocal and super-resolution light microscopy approaches for the users. The Zeiss LSM 710 laser scanning confocal microscope is equipped with 6 laser lines, and can provide resolution of 200 nm. The Zeiss Elyra S1 structured illumination microscope is equipped with one laser line (488 nm) and can provide resolution around 100 nm.

The unit can provide advice for sample preparation (preparation of live and fixed cells samples, expression and purification of cytoskeleton-associated proteins), as well as for sample labeling and optimal choice of the approaches.

Instruments:

  • Jobin Yvon Nanolog
  • Zeiss LSM 710 laser scanning confocal micorscope
  • Zeiss Elyra S1 structured illumination microscope
  • Thermo Science DXR Raman microscope

Related organizations:

  • Rutherford Appleton Laboratory
  • Central Laser Facility

Contact: Dr. András Lukács, andras.lukacs@aok.pte.hu

  • Zeiss, LSM 710 laser scanning confocal micorscope,
  • Zeiss Elyra S1 structured illumination microscope, 
  • Jobin Yon Nanolog, Thermo Science DXR Raman microscope

Molecular biophysics research group