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Journal of Bacteriology, February 2009, p. 728-734, Vol. 191, No. 3
0021-9193/09/$08.00+0     doi:10.1128/JB.01363-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Crystal Structure of ORF12 from Lactococcus lactis Phage p2 Identifies a Tape Measure Protein Chaperone{triangledown} ,{dagger}

Marina Siponen,1 Giuliano Sciara,1 Manuela Villion,2,4 Silvia Spinelli,1 Julie Lichière,1 Christian Cambillau,1 Sylvain Moineau,2,3,4* and Valérie Campanacci1*

Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités d'Aix-Marseille I & II, Campus de Luminy, case 932, 13288 Marseille cedex 09, France,1 Groupe de Recherche en Écologie Buccale (GREB), Faculté de Médecine Dentaire,2 Félix d'Hérelle Reference Center for Bacterial Viruses,3 Département de Biochimie et de Microbiologie, Faculté des Sciences et de Génie, Université Laval, Québec City, Québec, Canada G1K 7P44

Received 30 September 2008/ Accepted 20 November 2008

We report here the characterization of the nonstructural protein ORF12 of the virulent lactococcal phage p2, which belongs to the Siphoviridae family. ORF12 was produced as a soluble protein, which forms large oligomers (6- to 15-mers) in solution. Using anti-ORF12 antibodies, we have confirmed that ORF12 is not found in the virion structure but is detected in the second half of the lytic cycle, indicating that it is a late-expressed protein. The structure of ORF12, solved by single anomalous diffraction and refined at 2.9-Å resolution, revealed a previously unknown fold as well as the presence of a hydrophobic patch at its surface. Furthermore, crystal packing of ORF12 formed long spirals in which a hydrophobic, continuous crevice was identified. This crevice exhibited a repeated motif of aromatic residues, which coincided with the same repeated motif usually found in tape measure protein (TMP), predicted to form helices. A model of a complex between ORF12 and a repeated motif of the TMP of phage p2 (ORF14) was generated, in which the TMP helix fitted exquisitely in the crevice and the aromatic patches of ORF12. We suggest, therefore, that ORF12 might act as a chaperone for TMP hydrophobic repeats, maintaining TMP in solution during the tail assembly of the lactococcal siphophage p2.

* Corresponding author. Mailing address for Valérie Campanacci: Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités d'Aix-Marseille I & II, Campus de Luminy, case 932, 13288 Marseille cedex 09, France. Phone: 33 491 82 55 91. Fax: 33 491-266-720. E-mail: valerie.campanacci{at}afmb.univ-mrs.fr. Mailing address for Sylvain Moineau: Groupe de Recherche en Écologie Buccale (GREB), Faculté de Médecine Dentaire, Université Laval, Québec City, Québec, Canada G1K 7P4. Phone: (418) 656-3712. Fax: (418) 656-2861. E-mail: Sylvain.Moineau{at}bcm.ulaval.ca

{triangledown} Published ahead of print on 1 December 2008.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, February 2009, p. 728-734, Vol. 191, No. 3
0021-9193/09/$08.00+0     doi:10.1128/JB.01363-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Rousseau, G. M., Moineau, S. (2009). Evolution of Lactococcus lactis Phages within a Cheese Factory. Appl. Environ. Microbiol. 75: 5336-5344 [Abstract] [Full Text]  


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