Research - Core Facilities - Laboratory of Proteomics Research

Katalin MEDZIHRADSZKY
head, principal investigator

picture
Éva HUNYADI-GULYÁS research associate
Zsuzsanna DARULA research associate
Éva KLEMENT research associate
Ágnes BÁLÓNÉ ÁRVA technician
Hajnalka DÜRGŐ Ph.D. student

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 Centre 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 (nanoACQUITY UPLC system, Waters) 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.


Downloads:
Sample preparation for mass spectrometry

Selected publications

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.

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.

Darula Z, Medzihradszky KF. (2009). Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum.Mol Cell Proteomics. 8(11):2515-26.

Lipinszki Z, Kiss P, Pál M, Deák P, Szabó A, Hunyadi-Gulyas E, Klement E, Medzihradszky KF, Udvardy A. (2009). Developmental-stage-specific regulation of the polyubiquitin receptors in Drosophila melanogaster. J Cell Sci. 122(Pt 17):3083-92.

Klement E, Lipinszki Z, Kupihár Z, Udvardy A, Medzihradszky KF. (2010). Enrichment of O-GlcNAc modified proteins by the periodate oxidation-hydrazide resin capture approach. J Proteome Res. 9(5):2200-6.

Darula Z, Chalkley RJ, Baker P, Burlingame AL, Medzihradszky KF. (2010). Mass spectrometric analysis, automated identification and complete annotation of O-linked glycopeptides. Eur J Mass Spectrom. 16(3):421-8.

Raskó T, Dér A, Klement E, Slaska-Kiss K, Pósfai E, Medzihradszky KF, Marshak DR, Roberts RJ, Kiss A. (2010). BspRI restriction endonuclease: cloning, expression in Escherichia coli and sequential cleavage mechanism. Nucleic Acids Res. 38(20):7155-66.