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Báo cáo khoa học: How disorder influences order and vice versa – mutual effects in fusion proteins containing an intrinsically disordered and a globular protein

Intrinsically disordered proteins (IDPs) are functional proteins either fully or partly lacking stable secondary and tertiary structure under physiologi-cal conditions that are involved in important biological functions, such as regulation and signalling in eukaryotes, prokaryotes and viruses. | ễFEBS Journal How disorder influences order and vice versa - mutual effects in fusion proteins containing an intrinsically disordered and a globular protein Ilaria Sambi1 Pietro Gatti-Lafranconi1 Sonia Longhi2 and Marina Lotti1 1 Dipartimento di Biotecnologie e Bioscienze University di Milano-Bicocca Italy 2 Architecture et Fonction des Macromolecules Biologiques Universite Aix-Marseille I et II France Keywords conformation fusion proteins intrinsically disordered proteins stability viralproteins Correspondence M. Lotti Dipartimento di Biotecnologie e Bioscienze Universita di Milano-Bicocca Piazza della Scienza 2 20126 Milano Italy Fax 3902 6448 3569 Tel 3902 6448 3527 E-mail marina.lotti@unimib.it or S. Longhi Architecture et Fonction des Macromolecules Biologiques AFMB UMR 6098 CNRS et Universites d Aix-Marseille I et II 163 Avenue de Luminy Case 932 13288 Marseille Cedex 09 France Fax 33 0 4 91 26 67 20 Tel 33 0 4 91 82 55 80 E-mail sonia.longhi@afmb.univ-mrs.fr Intrinsically disordered proteins IDPs are functional proteins either fully or partly lacking stable secondary and tertiary structure under physiological conditions that are involved in important biological functions such as regulation and signalling in eukaryotes prokaryotes and viruses. The function of many IDPs relies upon interactions with partner proteins often accompanied by conformational changes and disorder-to-order transitions in the unstructured partner. To investigate how disordered and ordered regions interact when fused to one to another within the same protein we covalently linked the green fluorescent protein to three different well characterized IDPs and analyzed the conformational properties of the fusion proteins using various biochemical and biophysical approaches. We observed that the overall structure compactness and stability of the chimeric proteins all differ from what could have been anticipated from the structural features of their isolated components and that they vary as a .