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Interaction between the C-terminal domains of N and P proteins of measles virus investigated by NMR.

Bernard C, Gely S, Bourhis JM, Morelli X, Longhi S, Darbon H
FEBS Lett 583 1084-9 (2009)
Cited: 34 times
EuropePMC logo PMID: 19275899

Abstract

In this paper we investigate the interaction between the C-terminal domains of the measles virus phosphoprotein (XD) and nucleoprotein (N(TAIL)) by using nuclear magnetic resonance chemical shift perturbation experiments. Using both N(TAIL) constructs and peptides, we show that contrary to the conserved Box2 region (N(489-506)), the C-terminal region of N(TAIL) (N(513-525)) does not directly interact with XD, and yet affects binding to XD. We tentatively propose a model where the C-terminus of N(TAIL) would stabilize the N(TAIL)-XD complex either via a functional coupling with N(489-506) or by reducing the entropic penalty associated to the binding-coupled-to-folding process.

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Reviews citing this publication (3)

  1. Roles of intrinsic disorder in protein-nucleic acid interactions. Dyson HJ. Mol Biosyst 8 97-104 (2012)
  2. Structural disorder within paramyxovirus nucleoproteins and phosphoproteins. Habchi J, Longhi S. Mol Biosyst 8 69-81 (2012)
  3. Probing structural transitions in both structured and disordered proteins using site-directed spin-labeling EPR spectroscopy. Longhi S, Belle V, Fournel A, Guigliarelli B, Carrière F. J Pept Sci 17 315-328 (2011)

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  1. The matrix protein of measles virus regulates viral RNA synthesis and assembly by interacting with the nucleocapsid protein. Iwasaki M, Takeda M, Shirogane Y, Nakatsu Y, Nakamura T, Yanagi Y. J Virol 83 10374-10383 (2009)
  2. Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions. Liljeroos L, Huiskonen JT, Ora A, Susi P, Butcher SJ. Proc Natl Acad Sci U S A 108 18085-18090 (2011)
  3. Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein. Gely S, Lowry DF, Bernard C, Jensen MR, Blackledge M, Costanzo S, Bourhis JM, Darbon H, Daughdrill G, Longhi S. J Mol Recognit 23 435-447 (2010)
  4. Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. Habchi J, Mamelli L, Darbon H, Longhi S. PLoS One 5 e11684 (2010)
  5. Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. J Biol Chem 286 13583-13602 (2011)
  6. Conformational analysis of the partially disordered measles virus N(TAIL)-XD complex by SDSL EPR spectroscopy. Kavalenka A, Urbancic I, Belle V, Rouger S, Costanzo S, Kure S, Fournel A, Longhi S, Guigliarelli B, Strancar J. Biophys J 98 1055-1064 (2010)
  7. Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength. Bloyet LM, Brunel J, Dosnon M, Hamon V, Erales J, Gruet A, Lazert C, Bignon C, Roche P, Longhi S, Gerlier D. PLoS Pathog 12 e1006058 (2016)
  8. Binding of rabies virus polymerase cofactor to recombinant circular nucleoprotein-RNA complexes. Ribeiro Ede A, Leyrat C, Gérard FC, Albertini AA, Falk C, Ruigrok RW, Jamin M. J Mol Biol 394 558-575 (2009)
  9. Probing structural transitions in the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by vibrational spectroscopy of cyanylated cysteines. Bischak CG, Longhi S, Snead DM, Costanzo S, Terrer E, Londergan CH. Biophys J 99 1676-1683 (2010)
  10. Research Support, Non-U.S. Gov't Fuzzy regions in an intrinsically disordered protein impair protein-protein interactions. Gruet A, Dosnon M, Blocquel D, Brunel J, Gerlier D, Das RK, Bonetti D, Gianni S, Fuxreiter M, Longhi S, Bignon C. FEBS J 283 576-594 (2016)
  11. Phosphorylation of measles virus phosphoprotein at S86 and/or S151 downregulates viral transcriptional activity. Sugai A, Sato H, Yoneda M, Kai C. FEBS Lett 586 3900-3907 (2012)
  12. Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus. Shu Y, Habchi J, Costanzo S, Padilla A, Brunel J, Gerlier D, Oglesbee M, Longhi S. J Biol Chem 287 11951-11967 (2012)
  13. The structurally disordered paramyxovirus nucleocapsid protein tail domain is a regulator of the mRNA transcription gradient. Cox RM, Krumm SA, Thakkar VD, Sohn M, Plemper RK. Sci Adv 3 e1602350 (2017)
  14. Nipah and Hendra Virus Nucleoproteins Inhibit Nuclear Accumulation of Signal Transducer and Activator of Transcription 1 (STAT1) and STAT2 by Interfering with Their Complex Formation. Sugai A, Sato H, Takayama I, Yoneda M, Kai C. J Virol 91 e01136-17 (2017)
  15. Dynamics of the intrinsically disordered C-terminal domain of the nipah virus nucleoprotein and interaction with the x domain of the phosphoprotein as unveiled by NMR spectroscopy. Baronti L, Erales J, Habchi J, Felli IC, Pierattelli R, Longhi S. Chembiochem 16 268-276 (2015)
  16. Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling. D'Urzo A, Konijnenberg A, Rossetti G, Habchi J, Li J, Carloni P, Sobott F, Longhi S, Grandori R. J Am Soc Mass Spectrom 26 472-481 (2015)
  17. Structure of the nucleoprotein binding domain of Mokola virus phosphoprotein. Assenberg R, Delmas O, Ren J, Vidalain PO, Verma A, Larrous F, Graham SC, Tangy F, Grimes JM, Bourhy H. J Virol 84 1089-1096 (2010)
  18. Dissecting partner recognition by an intrinsically disordered protein using descriptive random mutagenesis. Gruet A, Dosnon M, Vassena A, Lombard V, Gerlier D, Bignon C, Longhi S. J Mol Biol 425 3495-3509 (2013)
  19. Biochemical and structural studies of the oligomerization domain of the Nipah virus phosphoprotein: evidence for an elongated coiled-coil homotrimer. Blocquel D, Beltrandi M, Erales J, Barbier P, Longhi S. Virology 446 162-172 (2013)
  20. Phosphorylation of measles virus nucleoprotein affects viral growth by changing gene expression and genomic RNA stability. Sugai A, Sato H, Yoneda M, Kai C. J Virol 87 11684-11692 (2013)
  21. Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: a tight complex implying one binding site. Blocquel D, Habchi J, Costanzo S, Doizy A, Oglesbee M, Longhi S. Protein Sci 21 1577-1585 (2012)
  22. One-step generation of error-prone PCR libraries using Gateway® technology. Gruet A, Longhi S, Bignon C. Microb Cell Fact 11 14 (2012)
  23. The feet of the measles virus polymerase bind the viral nucleocapsid protein at a single site. Yegambaram K, Kingston RL. Protein Sci 19 893-899 (2010)
  24. Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X Domain. Bonetti D, Camilloni C, Visconti L, Longhi S, Brunori M, Vendruscolo M, Gianni S. J Biol Chem 291 10886-10892 (2016)
  25. Newly identified minor phosphorylation site threonine-279 of measles virus nucleoprotein is a prerequisite for nucleocapsid formation. Sugai A, Sato H, Hagiwara K, Kozuka-Hata H, Oyama M, Yoneda M, Kai C. J Virol 88 1140-1149 (2014)
  26. Free ISG15 Inhibits the Replication of Peste des Petits Ruminants Virus by Breaking the Interaction of Nucleoprotein and Phosphoprotein. Tang J, Tang A, Jia N, Du H, Liu C, Zhu J, Li C, Meng C, Liu G. Microbiol Spectr 10 e0103122 (2022)
  27. Structures of the mumps virus polymerase complex via cryo-electron microscopy. Li T, Liu M, Gu Z, Su X, Liu Y, Lin J, Zhang Y, Shen QT. Nat Commun 15 4189 (2024)


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