The intrinsically disordered C‐terminal domain of the measles virus nucleoprotein interacts with the C‐terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded

Protein Science - Tập 14 Số 8 - Trang 1975-1992 - 2005
Jean‐Marie Bourhis1, Véronique Receveur‐Bréchot1, Michael Oglesbee2, Xinsheng Zhang2, Matthew Buccellato2, Hervé Darbon1, Bruno Canard1, Stéphanie Finet3, Sonia Longhi1
1Architecture et Fonction des Macromolé cules Biologiques (AFMB), UMR 6098 CNRS et Université s Aix-Marseille I et II, ESIL, Campus de Luminy, 13288 Marseille Cedex 09, France
2Department Veterinary Biosciences, The Ohio State University, Columbus, Ohio 43210, USA
3European Synchrotron Radiation Facility, BP 220, 38043 Grenoble Cedex, France

Tóm tắt

AbstractMeasles virus is a negative‐sense, single‐stranded RNA virus within theMononegavirales order,which includes several human pathogens, including rabies, Ebola, Nipah, and Hendra viruses. Themeasles virus nucleoprotein consists of a structured N‐terminal domain, and of an intrinsically disordered C‐terminal domain, NTAIL (aa 401–525), which undergoes induced folding in the presence of the C‐terminal domain (XD, aa 459–507) of the viral phosphoprotein. With in NTAIL, an α‐helical molecular recognition element (α‐MoRE, aa 488–499) involved in binding to P and in induced folding was identified and then observed in the crystal structure of XD. Using small‐angle X‐ray scattering, we have derived a low‐resolution structural model of the complex between XD and NTAIL, which shows that most of NTAIL remains disordered in the complex despite P‐induced folding within the α‐MoRE. The model consists of an extended shape accommodating the multiple conformations adopted by the disordered N‐terminal region of NTAIL, and of a bulky globular region, corresponding to XD and to the C terminus of NTAIL (aa 486–525). Using surface plasmon resonance, circular dichroism, fluorescence spectroscopy, and heteronuclear magnetic resonance, we show that NTAIL has an additional site (aa 517–525) involved in binding to XD but not in the unstructured‐to‐structured transition. This work provides evidence that intrinsically disordered domains can establish complex interactions with their partners, and can contact them through multiple sites that do not all necessarily gain regular secondary structure.

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Tài liệu tham khảo

10.1006/viro.1996.0060

10.1107/S0021889800008372

10.1016/S0965-1748(01)00171-0

10.1021/bi015763t

10.1016/j.virusres.2003.11.007

Brizzard B.L., 1994, Immunoaffinity purification of FLAG epitope‐tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution, Biotechniques, 16, 730

10.1128/jvi.67.10.5803-5812.1993

10.1099/0022-1317-70-2-435

10.1128/JVI.75.3.1117-1123.2001

10.1021/bi047817f

10.1006/viro.1996.0359

10.1016/S0065-3527(08)60373-5

Curran J., 1993, The hypervariable C‐terminal tail of the Sendai paramyxovirus nucleocapsid protein is required for template function but not for RNA encapsidation, J. Virol., 67, 4358, 10.1128/jvi.67.7.4358-4364.1993

10.1006/viro.1994.1409

10.1006/viro.1995.9946

Curran J., 1995, An N‐terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication, J. Virol., 69, 849, 10.1128/jvi.69.2.849-855.1995

10.1002/(SICI)1097-0029(19991015)47:2<114::AID-JEMT4>3.0.CO;2-E

10.1074/jbc.M310348200

10.1099/0022-1317-75-1-233

10.1038/nbt0901-805

10.1016/S1093-3263(00)00138-8

10.1038/nrm1589

10.1128/JVI.73.7.5852-5864.1999

10.1021/bi972494r

10.1016/j.jmb.2004.03.017

10.1016/0168-1702(88)90011-1

Guinier A., 1955, Small angle scattering of X‐rays

10.1074/jbc.M307036200

10.1099/0022-1317-76-11-2863

10.1073/pnas.77.5.2631

10.1016/0042-6822(81)90235-X

10.1021/bi9800808

10.1074/jbc.M308745200

10.1006/viro.2002.1634

10.1006/viro.2001.1296

10.1099/vir.0.19451-0

10.1073/pnas.0402690101

10.1128/JVI.78.16.8630-8640.2004

10.1107/S0021889800014126

10.1038/nsmb746

10.1128/JVI.77.21.11332-11346.2003

10.1099/vir.0.80791-0

Lamb R.A., 2001, Fields virology, 1305

10.1016/0168-1702(95)00067-Z

10.1007/s007050050078

10.1074/jbc.M300518200

10.1016/S1097-2765(01)80003-4

10.1111/j.1574-6968.2001.tb10889.x

10.1006/jmrb.1995.1109

10.1002/(SICI)1099-1387(199906)5:6<263::AID-PSC191>3.0.CO;2-A

10.1099/0022-1317-71-4-775

10.1021/bi9707180

10.1006/viro.1996.8429

10.1099/0022-1317-80-6-1383

10.1016/S0168-9002(01)00553-8

10.1099/0022-1317-70-9-2409

10.1002/prot.10481

10.1007/BF02192855

10.1016/S0092-8674(00)80463-8

10.1046/j.1365-2958.1998.00899.x

10.1074/jbc.M400673200

10.1159/000149074

10.1099/0022-1317-47-2-301

10.1016/S0076-6879(96)66033-9

10.1006/viro.1994.1331

Stallcup K.C., 1979, Purification of measles virus and characterization of subviral components, J. Virol., 30, 166, 10.1128/jvi.30.1.166-176.1979

10.1107/S0021889892001663

10.1107/S0021889895007047

10.1016/S0006-3495(01)76260-1

10.1038/79013

10.1128/JVI.76.8.3659-3669.2002

10.1016/S0968-0004(02)02169-2

10.1128/JVI.76.1.68-77.2002

10.1021/bi00211a042

10.1110/ps.4210102

10.1128/JVI.76.12.6121-6130.2002

10.1006/jmbi.1999.3110

10.1128/JVI.76.17.8737-8746.2002

10.1016/j.virol.2005.03.035

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Protein Science

Tập 14 Số 8

1975-1992

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