Production and characterisation of Epstein-Barr virus helicase-primase complex and its accessory protein BBLF2/3.

Abstract : The helicase-primase complex is part of the lytic DNA replication machinery of herpesviruses, but up to now, almost nothing is known about its structure. For Epstein-Barr virus it consists in the helicase BBLF4, the primase BSLF1 and the accessory protein BBLF2/3. The accessory protein shows only weak sequence homology within the herpesvirus family but may be related to an inactive B-family polymerase. BSLF1 belongs to the archaeo-eukaryotic primase family, whereas the helicase BBLF4 has been related either to Dda helicases of caudovirales or to Pif1 helicases. We produced the helicase-primase complex in insect cells using a baculovirus coding for all three proteins simultaneously. The soluble monomeric helicase-primase complex containing the three proteins with 1:1:1 stoichiometry showed ATPase activity, which is strongly stimulated in the presence of ssDNA oligomers. Furthermore, we expressed BBLF2/3 as soluble monomeric protein and performed small-angle X-ray scattering experiments which yielded an envelope whose shape is compatible with B-family polymerases.
Type de document :
Article dans une revue
Virus Genes, Springer Verlag, 2015, 51 (2), pp.171-81
Liste complète des métadonnées

http://hal.univ-grenoble-alpes.fr/hal-01243634
Contributeur : Frank Thomas <>
Soumis le : mardi 15 décembre 2015 - 11:26:14
Dernière modification le : jeudi 11 janvier 2018 - 06:21:39

Identifiants

  • HAL Id : hal-01243634, version 1
  • PUBMED : 26292944

Collections

Citation

Eric Thierry, Martha Brennich, Adam Round, Marlyse Buisson, Wim P Burmeister, et al.. Production and characterisation of Epstein-Barr virus helicase-primase complex and its accessory protein BBLF2/3.. Virus Genes, Springer Verlag, 2015, 51 (2), pp.171-81. 〈hal-01243634〉

Partager

Métriques

Consultations de la notice

95