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Szütsné Tóth Mónika Ágnes
Structural features of a disordered protein motif

Aug 29 - kedd

15:30 – 17:00

I. Poszterszekció

P30

Structural features of a disordered protein motif

Mónika Ágnes Tóth1, Péter Gaszler1, 3, Andrea Vig1, Veronika Takács-Kollár1, Illés Csonka2, Tamás Huber1, 3, Rauan Sakenov1, Réka Pintér1, Beáta Bugyi1, 3

1University of Pécs, Medical School, Department of Biophysics, Pécs Szigeti str 12. H-7624

2Lajos Nagy High School of the Cistercian Order

3Regional Committee of The Hungarian Academy of Sciences at Pécs, The Expert Committee of Physics and Astronomy, Spectroscopy Committee, Pécs, Hungary

SALS (sarcomere length short) is a Drosophila-specific sarcomeric protein that regulates sarcomere length and organization. Lack of SALS is lethal in embryonic age, possibly due to the shortening of sarcomeric actin filament length or the disruption of their order.

Our bioinformatics analysis suggests that SALS is an intrinsically disordered protein (IDP). IDPs are biologically active proteins, however, do not have a well-defined three-dimensional structure. They possess specific physicochemical properties different from those characteristics for ordered proteins (e.g., amino acid composition, thermal stability, electrophoretic mobility). There is growing attention to studying IDPs for their key roles in diseases or cellular processes. SALS contains two intrinsically disordered protein regions (IDRs), the Wiscott-Aldrich syndrome homology 2 (WH2) domains, composed of a few tens of amino acids. Proteins containing WH2 domains possess actin-binding properties and can exhibit multifunctional character depending on the number and sequence of WH2 domains.

Based on our functional analysis of the SALS WH2 domains (SALS-WH2), both WH2 domains interact with actin and influence actin homeostasis by shifting the monomer:filament ratio towards monomeric actin. The structural properties and conformational dynamics of SALS-WH2 have not yet been described. Therefore, we further aim to characterise these features using in silico and experimental approaches. Our prediction-based results were experimentally verified by fluorescence spectroscopy and thermal analysis.

Acknowledgements

This work was supported by ÚNKP-21-3-II-PTE-997 (PG), University of Pécs, Medical School (MÁT), 2021-4.1.2-NEMZ_KI-2022-00025 (TH). We thank József Mihály (Institute of Genetics, Biological Research Centre, Szeged) for the SALS plasmid.