DynaMo Seminar: Peter Tompa

DynaMo Center of Excellence is pleased to invite you to the second DynaMo Seminar. Our speaker is Peter Tompa from VIB Department of Structural Biology, Brussels, and Institute of Enzymology, Budapest.

The role of structural disorder in unusual protein-protein interactions

Structural view of fuzziness in protein–proteininteractions.

Abstract
Intrinsically disordered proteins (IDPs) have received increased attention lately, as it has become clear that the lack of a stable 3D structure is prevalent in the proteomes of higher organisms. Structural disorder is particularly prevalent in regulatory and signaling proteins, and IDPs often carry out their functions via protein-protein interactions (PPIs). After a short outline of the field, Peter Tompa will present results on the non-conventional involvement of disorder in PPIs. He will show that IDPs either interact with their partner via short linear motifs [1, 2] or domains [3], which often  have a strong preference for their structures attained in the bound state. This fine balance between order and disorder is probably indicative of the thermodynamic and kinetic fine-tuning of recognition by IDPs, in line with their preferential functioning in interaction networks. His studies suggest that IDPs use a much higher proportion of their residues for interaction than their globular counterparts, and they tend to expose their hydrophobic residues for effective interaction with their partners [4]. Whereas these observations can be interpreted in terms of induced folding that result in complexes with well-defined structures, the interactions of IDPs often have unusual structural-functional consequences, such as promiscuous functions (moonlighting [5]) and structural disorder in the bound state (fuzziness [6]).

Resume
The research of Peter Tompa focuses on intrinsically disordered proteins (IDPs). He played an active and decisive role in the rise of this field (cf. http://tompa.enzim.hu/) by suggesting a functional classification of IDPs, observing the role of structural disorder in chaperone function and developing basic concepts of the unusual modes of function of IDPs (moonlighting, fuzziness and disordered domains). Peter Tompa published more than 100 papers (about 40 of which are related to structural disorder), 10 book chapters, and the first monograph of the field “Structure and function of intrinsically disordered proteins” (2009) by Taylor and Francis, Inc (CRC Press). Peter Tompa has been an invited speaker at more than 70 international meetings, such as the first IDP subgroup meeting at the “51st Annual Meeting of the Biophysical Society” in Baltimore, USA (2007). He organized the first conference of the IDP field, the EMBO workshop “Intrinsically unfolded proteins: from structure to function” in Budapest, Hungary (2007), and chaired the second Gordon Research Conference on IDPs, in Vest Dover, VT, USA (2012). He holds a position of professor of biochemistry and protein sciences in the Institute of Enzymology of the Hungarian Academy of Sciences, Budapest, Hungary. Since May 1, 2011, he is also the director of VIB (Flanders Institute of Biotechnology) Department of Structural Biology, Brussels, and also a professor at the VUB (Free University Brussels). He has research groups both in Budapest and Brussels.



1.    Fuxreiter, M., et al. (2004) Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J Mol Biol 338: 1015-26.
2.    Fuxreiter, M., P. Tompa, and I. Simon (2007) Local structural disorder imparts plasticity on linear motifs. Bioinformatics 23: 950-6.
3.    Tompa, P., et al. (2009) Close encounters of the third kind: disordered domains and the interactions of proteins. Bioessays. 31: 328-35.
4.    Mészáros, B., et al. (2007) Molecular principles of the interactions of disordered proteins. J Mol Biol 372: 549-561.
5.    Tompa, P., C. Szasz, and L. Buday (2005) Structural disorder throws new light on moonlighting. Trends Biochem Sci 30: 484-9.
6.    Tompa, P. and M. Fuxreiter (2008) Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem Sci 33: 2-8.

Everybody is most welcome!