Experimental Characterization of Fuzzy Protein Assemblies: Interactions of Paramyxoviral NTAIL Domains With Their Functional Partners

被引:6
|
作者
Troilo, Francesca [1 ,2 ,3 ,4 ]
Bignon, Christophe [1 ,2 ]
Gianni, Stefano [3 ,4 ]
Fuxreiter, Monika [5 ]
Longhi, Sonia [1 ,2 ]
机构
[1] CNRS, Marseille, France
[2] Aix Marseille Univ, Lab Architecture & Fonct Macromol Biol AFMB, Marseille, France
[3] Sapienza Univ Roma, Dipartimento Sci Biochim A Rossi Fanelli, Ist Pasteur, Fdn Cenci Bolognetti, Rome, Italy
[4] Sapienza Univ Roma, Consiglio Nazl Ric, Ist Biol & Patol Mol, Rome, Italy
[5] Univ Debrecen, Dept Biochem & Mol Biol, MTA DE Lab Prot Dynam, Debrecen, Hungary
来源
关键词
C-TERMINAL DOMAIN; MEASLES-VIRUS NUCLEOPROTEIN; INTRINSICALLY DISORDERED PROTEIN; VESICULAR STOMATITIS-VIRUS; MOLECULAR RECOGNITION ELEMENT; RESIDUAL DIPOLAR COUPLINGS; TAIL-XD COMPLEX; STRUCTURAL DISORDER; CRYSTAL-STRUCTURE; N-TAIL;
D O I
10.1016/bs.mie.2018.08.006
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
In this chapter we detail various experimental approaches to characterize the fuzziness of complexes made of the C-terminal domain of the nucleoprotein (NTAIL) 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 NTAIL-XD complexes are characterized by a considerable amount of conformational heterogeneity. We also detail recent data that revealed that NTAIL is highly malleable, i. e., it displays a partner-mediated polymorphism. All the results suggest that NTAIL plasticity and fuzziness play a role in the coordination and regulation of the NTAIL interaction network so as to ensure efficient transcription and replication.
引用
收藏
页码:137 / 192
页数:56
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