1. The Opening of the SPP1 Bacteriophage Tail, a Prevalent Mechanism in Gram-positive-infecting Siphophages
- Author
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Paulo Tavares, Dale A. Shepherd, Julie Lichière, Eric Richard, Patrick Bron, David Veesler, Joséphine Lai-Kee-Him, Isabelle Auzat, Alison E. Ashcroft, Christian Cambillau, Gautier Robin, Adeline Goulet, Architecture et fonction des macromolécules biologiques (AFMB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Imagerie Moléculaire et Nanobiotechnologies - Institut Européen de Chimie et Biologie (IECB), Université Sciences et Technologies - Bordeaux 1-Centre National de la Recherche Scientifique (CNRS), Department of Biochemistry [Washington ], University of Washington [Seattle], Virologie moléculaire et structurale (VMS), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Institut de recherche en cancérologie de Montpellier (IRCM - U896 Inserm - UM1), CRLCC Val d'Aurelle - Paul Lamarque-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 1 (UM1), Astbury Centre for Structural Molecular Biology, University of Leeds, Laboratoire Frank Duncombe, Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Lab Virol Mol & Struct, Ctr Rech Gif, UPR 3296, Centre National de la Recherche Scientifique (CNRS), Centre de Biochimie Structurale [Montpellier] (CBS), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
Viral protein ,[SDV]Life Sciences [q-bio] ,Virus Attachment ,Trimer ,Genome, Viral ,Siphoviridae ,medicine.disease_cause ,Biochemistry ,Bacteriophage ,chemistry.chemical_compound ,Protein structure ,medicine ,Molecular Biology ,ComputingMilieux_MISCELLANEOUS ,Viral Structural Proteins ,biology ,Cell Biology ,biology.organism_classification ,Protein Structure, Tertiary ,N-terminus ,Crystallography ,chemistry ,Protein Structure and Folding ,biology.protein ,Biophysics ,DNA ,Catabolite activator protein ,Bacillus subtilis - Abstract
The SPP1 siphophage uses its long non-contractile tail and tail tip to recognize and infect the Gram-positive bacterium Bacillus subtilis. The tail-end cap and its attached tip are the critical components for host recognition and opening of the tail tube for genome exit. In the present work, we determined the cryo-electron microscopic (cryo-EM) structure of a complex formed by the cap protein gp19.1 (Dit) and the N terminus of the downstream protein of gp19.1 in the SPP1 genome, gp21(1-552) (Tal). This complex assembles two back-to-back stacked gp19.1 ring hexamers, interacting loosely, and two gp21(1-552) trimers interacting with gp19.1 at both ends of the stack. Remarkably, one gp21(1-552) trimer displays a "closed" conformation, whereas the second is "open" delineating a central channel. The two conformational states dock nicely into the EM map of the SPP1 cap domain, respectively, before and after DNA release. Moreover, the open/closed conformations of gp19.1-gp21(1-552) are consistent with the structures of the corresponding proteins in the siphophage p2 baseplate, where the Tal protein (ORF16) attached to the ring of Dit (ORF15) was also found to adopt these two conformations. Therefore, the present contribution allowed us to revisit the SPP1 tail distal-end architectural organization. Considering the sequence conservation among Dit and the N-terminal region of Tal-like proteins in Gram-positive-infecting Siphoviridae, it also reveals the Tal opening mechanism as a hallmark of siphophages probably involved in the generation of the firing signal initiating the cascade of events that lead to phage DNA release in vivo.
- Published
- 2011