Troilo Francesca, Bignon Christophe, Gianni Stefano, Fuxreiter Monika, Longhi Sonia
CNRS and Aix-Marseille Univ, Laboratoire Architecture et Fonction des Macromolecules Biologiques (AFMB), Marseille, France; Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli' and Istituto di Biologia e Patologia Molecolari del Consiglio Nazionale delle Ricerche, Sapienza Università di Roma, Rome, Italy.
CNRS and Aix-Marseille Univ, Laboratoire Architecture et Fonction des Macromolecules Biologiques (AFMB), Marseille, France.
Methods Enzymol. 2018;611:137-192. doi: 10.1016/bs.mie.2018.08.006. Epub 2018 Oct 5.
In this chapter we detail various experimental approaches to characterize the fuzziness of complexes made of the C-terminal domain of the nucleoprotein (N) from three representative paramyxoviruses and of the C-terminal X domain (XD) of the homologous phosphoprotein. We discuss the advantages, the limitations, as well as the caveats of the various methods. We describe experimental data showing that paramyxoviral N-XD complexes are characterized by a considerable amount of conformational heterogeneity. We also detail recent data that revealed that N is highly malleable, i.e., it displays a partner-mediated polymorphism. All the results suggest that N plasticity and fuzziness play a role in the coordination and regulation of the N interaction network so as to ensure efficient transcription and replication.
在本章中，我们详细介绍了各种实验方法，以表征来自三种代表性副粘病毒的核蛋白（N）的C末端结构域以及同源磷蛋白的C末端X结构域（XD）所形成复合物的模糊性。我们讨论了各种方法的优点、局限性以及注意事项。我们描述了实验数据，这些数据表明副粘病毒N-XD复合物具有相当程度的构象异质性。我们还详细介绍了最近的数据，这些数据揭示了N具有高度的可塑性，即它表现出伴侣介导的多态性。所有结果表明，N的可塑性和模糊性在N相互作用网络的协调和调节中发挥作用，以确保高效的转录和复制。
