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Institute of Plant Biology
- Laboratory of Plant Chrono- and Photobiology
- Laboratory of Molecular Stress- and Photobiology
- Laboratory of Photosynthetic Membranes
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- Laboratory of Plant Cell Division Cycle and Stress Adaptation
- Laboratory of Molecular Regulators of Plant Growth
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Katalin F. MEDZIHRADSZKY
Head,
Principal Investigator
| Éva HUNYADI-GULYÁS | Staff Scientist |
| Zsuzsanna DARULA | Staff Scientist |
| Éva KLEMENT | Staff Scientist |
| Hajnalka GYŐRI-DÜRGŐ | Technician |
| Ágnes BÁLÓNÉ ÁRVA | Technician |
LABORATORY OF PROTEOMICS RESEARCH
Proteomics research has become one of the most dynamic research areas. Well equipped Proteomics Centers have been established all over the world. Investigating the proteome provides answers to exciting questions, such as, which genes are transcribed and eventually translated; in what form are these proteins biologically active; which other proteins they interact with; how are these processes controlled etc. Mass spectrometry has become the method of choice for proteomics research. It is equally well suitable for protein identification, de novo sequencing, for the characterization of post-translational modifications, or other covalent labeling. It also can be utilized for investigating the 3D structure of proteins as well as the spatial organization of protein complexes. Last but not least, besides the qualitative characterization of the proteome mass spectrometry can also deliver quantitative results.
We have extensive collaborations within the Biological Research Center and with academic organizations in Hungary and abroad. Biological samples are provided by our collaborative partners. Our tasks are the analytical sample preparation, chromatographic fractionation if necessary, mass spectrometry analysis as well as data interpretation. Obviously we provide identifications for 1D- or 2D-gel isolated proteins. We have been involved in the characterization of disulfide-bridges, preoteolytic cleavage sites, phosphorylation as well as ubiquitination. We have been developing novel analytical methods for the characterization of secreted as well as intracellular O-glycosylation.
We also provide services for a fee: protein identification as well as mass measurements.
Our resources: analytical HPLC system for sample preparations; a nanoHPLC system, equipped with an autosampler (SunChrom/Eldex) coupled with an LCQ Fleet 3D ion trap (Thermo Fischer Scientific); a Reflex III MALDI-TOF MS (Bruker); and a nanoACQUITY UPLC system coupled with a Q-TOF Premier mass spectrometer (Waters) (the latter two are shared with the researchers of the Szeged University); in-house Mascot and ProteinProspector servers.
Selected publications
Hunyadi-Gulyas, E. and Medzihradszky, K.F. (2004). Factors that contribute to the complexity of protein digests. Drug Discovery Today 3: S3-S10.
Bekesi, A., Zagyva, I., Hunyadi Gulyas, E., Pongracz, V., Kovari, J., Nagy, A.O., Erdei, A., Medzihradszky, K.F. and Vertessy, B.G. (2004). Developmental regulation of dUTPase in Drosophila melanogaster. J. Biol. Chem. 279: 22362-22370.
Medzihradszky, K.F., Darula, Z., Perlson, E., Fainzilber, M., Chalkley, R.J., Ball, H., Greenbaum, D., Bogyo, M., Tyson, D.R., Bradshaw, R.A. and Burlingame, A.L. (2004). O-sulfonation of serine and threonine - Mass spectrometric detection and characterization of a new posttranslational modification in diverse proteins throughout the eukaryotes. Mol. Cell. Proteomics 3: 429-440.
Csizmok, V., Bokor, N., Banki, P., Klement, E., Medzihradszky, K.F., Friedrich, P., Tompa, K.A. and Tompa, P. (2005). Primary contact sites in intrinsically unstructured proteins: The case of calpastatin and microtubule-associated protein 2. Biochemistry-US 44: 3955-3964.
Ott, P.G., Varga, G.J., Szatmari, A., Bozso, Z., Klement, E., Medzihradszky, K.F., Besenyei, E., Czelleng, A. and Klement, Z. (2006). Novel extracellular chitinases rapidly and specifically induced by general bacterial elicitors and suppressed by virulent bacteria as a marker of early basal resistance in tobacco. Mol. Plant Microbe Interact. 19: 161-172.
Kurucz, E., Markus, R., Zsamboki, J., Folkl Medzihradszky, K., Darula, Z., Vilmos, P., Udvardy, A., Krausz, I., Lukacsovich, T., Gateff, E., Zettervall, C.J., Hultmark, D. and Ando, I. (2007). Nimrod, a putative phagocytosis receptor with EGF repeats in Drosophila plasmatocytes. Curr. Biol. 17: 649-654.
Kiss, A., Baliko, G., Csorba, A., Chuluunbaatar, T., Medzihradszky, K.F. and Alfoldi, L. (2008). Cloning and characterization of the DNA region responsible for megacin A- 216 production in Bacillus megaterium 216. J. Bacteriol. 190: 6448-6457.
Szajli, E., Feher, T. and Medzihradszky, K.F. (2008). Investigating the quantitative nature of MALDI-TOF MS. Mol. Cell. Proteomics 7: 2410-2418.
Szollosi, E., Bokor, M., Bodor, A., Perczel, A., Klement, E., Medzihradszky, K.F., Tompa, K. and Tompa, P. (2008). Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities. J. Proteome Res. 7: 2291-2299.
Zsigmond, L., Rigo, G., Szarka, A., Szekely, G., Otvos, K., Darula, Z., Medzihradszky, K,F., Koncz, C., Koncz, Z. and Szabados, L. (2008). Arabidopsis PPR40 connects abiotic stress responses to mitochondrial electron transport. Plant Physiol. 146: 1721-1737.