Research - Laboratories of Core Facilities - Laboratory of Proteomics Research

senior research associate

Éva HUNYADI-GULYÁS senior research associate
Zsuzsanna DARULA senior research associate
Éva KLEMENT research associate
Aladár PETTKÓ-SZANDTNER research associate
Ádám PAP PhD student
Ágnes BÁLÓNÉ ÁRVA laboratory assistant


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 Reflex III MALDI-TOF MS (Bruker); a nanoHPLC system, equipped with an autosampler (SunChrom) coupled with an LCQ Fleet 3D ion trap (Thermo Fischer Scientific); and a nanoACQUITY UPLC system (Waters) coupled with an LTQ-Orbitrap Elite (Thermo Fischer Scientific) (the latter is shared with the lipidomics researchers of the Laboratory of Molecular Stress Biology); in-house Mascot and Protein Prospector servers.

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.

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.

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.

Lipinszki Z, Pál M, Nagy O, Deák P, Hunyadi-Gulyas E, Udvardy A. (2011) Overexpression of Dsk2/dUbqln results in severe developmental defects and lethality in Drosophila melanogaster that can be rescued by overexpression of the p54/Rpn10/S5a proteasomal subunit. FEBS J. 278(24):4833-44.

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.

Darula Z, Sherman J, Medzihradszky KF. (2012) How to dig deeper? Improved enrichment methods for mucin core-1 type glycopeptides. Mol Cell Proteomics. 11(7):O111.016774.

Medzihradszky KF, Bohlen CJ. (2012) Partial de novo sequencing and unusual CID fragmentation of a 7 kDa, disulfide-bridged toxin. J Am Soc Mass Spectrom. 23(5):923-34.

Fekete A, Kenesi E, Hunyadi-Gulyas E, Durgo H, Berko B, Dunai ZA, Bauer PI. (2012) The guanine-quadruplex structure in the human c-myc gene's promoter is converted into B-DNA form by the human poly(ADP-ribose)polymerase-1. PLoS One. 2012;7(8):e42690.

Medzihradszky M, Bindics J, Adám E, Viczián A, Klement E, Lorrain S, Gyula P, Mérai Z, Fankhauser C, Medzihradszky KF, Kunkel T, Schäfer E, Nagy F. (2013). Phosphorylation of Phytochrome B Inhibits Light-Induced Signaling via Accelerated Dark Reversion in Arabidopsis. Plant Cell. 25(2):535-44.

Rigó G, Ayaydina F, Tietzb O, Zsigmond L, Kovács H, Páy A, Salchert K, Darula Z, Medzihradszky KF, Szabados L, Palme K, Koncz C, Cséplő A. (2013) Inactivation of plasma-membrane localized CDPK-related kinase 5 decelerates PIN2 exocytosis and root gravitropic response. Plant Cell. 25(5):1592-608.