Interaction of packaging motor with the polymerase complex of dsRNA bacteriophage

Jiri Lisal, Denis E Kainov, TuKiet T Lam, Mark R Emmett, Hui Wei, Paul Gottlieb, Alan G Marshall, Roman Tuma

    Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

    Sammanfattning

    Many viruses employ molecular motors to package their genomes into preformed empty capsids (procapsids). In dsRNA bacteriophages the packaging motor is a hexameric ATPase P4, which is an integral part of the multisubunit procapsid. Structural and biochemical studies revealed a plausible RNA-translocation mechanism for the isolated hexamer. However, little is known about the structure and regulation of the hexamer within the procapsid. Here we use hydrogen-deuterium exchange and mass spectrometry to delineate the interactions of the P4 hexamer with the bacteriophage phi12 procapsid. P4 associates with the procapsid via its C-terminal face. The interactions also stabilize subunit interfaces within the hexamer. The conformation of the virus-bound hexamer is more stable than the hexamer in solution, which is prone to spontaneous ring openings. We propose that the stabilization within the viral capsid increases the packaging processivity and confers selectivity during RNA loading. (c) 2006 Elsevier Inc. All rights reserved.
    Originalspråkengelska
    TidskriftVirology
    Volym351
    Sidor (från-till)73-79
    Antal sidor7
    ISSN0042-6822
    DOI
    StatusPublicerad - 2006
    MoE-publikationstypA1 Tidskriftsartikel-refererad

    Citera det här

    Lisal, J., Kainov, D. E., Lam, T. T., Emmett, M. R., Wei, H., Gottlieb, P., ... Tuma, R. (2006). Interaction of packaging motor with the polymerase complex of dsRNA bacteriophage. Virology, 351, 73-79. https://doi.org/10.1016/j.virol.2006.03.025
    Lisal, Jiri ; Kainov, Denis E ; Lam, TuKiet T ; Emmett, Mark R ; Wei, Hui ; Gottlieb, Paul ; Marshall, Alan G ; Tuma, Roman. / Interaction of packaging motor with the polymerase complex of dsRNA bacteriophage. I: Virology. 2006 ; Vol. 351. s. 73-79.
    @article{5274553d867140cc8e2ca869b38fb4eb,
    title = "Interaction of packaging motor with the polymerase complex of dsRNA bacteriophage",
    abstract = "Many viruses employ molecular motors to package their genomes into preformed empty capsids (procapsids). In dsRNA bacteriophages the packaging motor is a hexameric ATPase P4, which is an integral part of the multisubunit procapsid. Structural and biochemical studies revealed a plausible RNA-translocation mechanism for the isolated hexamer. However, little is known about the structure and regulation of the hexamer within the procapsid. Here we use hydrogen-deuterium exchange and mass spectrometry to delineate the interactions of the P4 hexamer with the bacteriophage phi12 procapsid. P4 associates with the procapsid via its C-terminal face. The interactions also stabilize subunit interfaces within the hexamer. The conformation of the virus-bound hexamer is more stable than the hexamer in solution, which is prone to spontaneous ring openings. We propose that the stabilization within the viral capsid increases the packaging processivity and confers selectivity during RNA loading. (c) 2006 Elsevier Inc. All rights reserved.",
    author = "Jiri Lisal and Kainov, {Denis E} and Lam, {TuKiet T} and Emmett, {Mark R} and Hui Wei and Paul Gottlieb and Marshall, {Alan G} and Roman Tuma",
    year = "2006",
    doi = "10.1016/j.virol.2006.03.025",
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    Lisal, J, Kainov, DE, Lam, TT, Emmett, MR, Wei, H, Gottlieb, P, Marshall, AG & Tuma, R 2006, 'Interaction of packaging motor with the polymerase complex of dsRNA bacteriophage', Virology, vol. 351, s. 73-79. https://doi.org/10.1016/j.virol.2006.03.025

    Interaction of packaging motor with the polymerase complex of dsRNA bacteriophage. / Lisal, Jiri; Kainov, Denis E; Lam, TuKiet T; Emmett, Mark R; Wei, Hui; Gottlieb, Paul; Marshall, Alan G; Tuma, Roman.

    I: Virology, Vol. 351, 2006, s. 73-79.

    Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

    TY - JOUR

    T1 - Interaction of packaging motor with the polymerase complex of dsRNA bacteriophage

    AU - Lisal, Jiri

    AU - Kainov, Denis E

    AU - Lam, TuKiet T

    AU - Emmett, Mark R

    AU - Wei, Hui

    AU - Gottlieb, Paul

    AU - Marshall, Alan G

    AU - Tuma, Roman

    PY - 2006

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    N2 - Many viruses employ molecular motors to package their genomes into preformed empty capsids (procapsids). In dsRNA bacteriophages the packaging motor is a hexameric ATPase P4, which is an integral part of the multisubunit procapsid. Structural and biochemical studies revealed a plausible RNA-translocation mechanism for the isolated hexamer. However, little is known about the structure and regulation of the hexamer within the procapsid. Here we use hydrogen-deuterium exchange and mass spectrometry to delineate the interactions of the P4 hexamer with the bacteriophage phi12 procapsid. P4 associates with the procapsid via its C-terminal face. The interactions also stabilize subunit interfaces within the hexamer. The conformation of the virus-bound hexamer is more stable than the hexamer in solution, which is prone to spontaneous ring openings. We propose that the stabilization within the viral capsid increases the packaging processivity and confers selectivity during RNA loading. (c) 2006 Elsevier Inc. All rights reserved.

    AB - Many viruses employ molecular motors to package their genomes into preformed empty capsids (procapsids). In dsRNA bacteriophages the packaging motor is a hexameric ATPase P4, which is an integral part of the multisubunit procapsid. Structural and biochemical studies revealed a plausible RNA-translocation mechanism for the isolated hexamer. However, little is known about the structure and regulation of the hexamer within the procapsid. Here we use hydrogen-deuterium exchange and mass spectrometry to delineate the interactions of the P4 hexamer with the bacteriophage phi12 procapsid. P4 associates with the procapsid via its C-terminal face. The interactions also stabilize subunit interfaces within the hexamer. The conformation of the virus-bound hexamer is more stable than the hexamer in solution, which is prone to spontaneous ring openings. We propose that the stabilization within the viral capsid increases the packaging processivity and confers selectivity during RNA loading. (c) 2006 Elsevier Inc. All rights reserved.

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