Bacteriophage SPP1 Tail Tube Protein Self-assembles into β-Structure-rich Tubes

Langlois, Chantal; Ramboarina, Stephanié; Cukkemane, Abhishek; Auzat, Isabelle; Chagot, Benjamin; Gilquin, Bernard; Ignatiou, Athanasios; Petitpas, I.; Kasotakis, Emmanouil; Paternostre, Maı̈té; White, Helen; Orlova, Elena V.; Baldus, Marc; Tavares, Paulo; Zinn‐Justin, Sophie

doi:10.1074/jbc.m114.613166

Cited by 28 publications

(51 citation statements)

References 41 publications

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“…The capsid-distal region of the tail features an adsorption apparatus. Binding of this apparatus to the host cell receptor YueB (17, 18) triggers a domino-like cascade of conformational changes within the gp17.1/gp17.1* tail tube (7,16,19), signaling for opening of the gp16 stopper to initiate delivery of the SPP1 genome to the host cell.…”

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confidence: 99%

Structural rearrangements in the phage head-to-tail interface during assembly and infection

Chaban

Lurz

Brasilès

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Many icosahedral viruses use a specialized portal vertex to control genome encapsidation and release from the viral capsid. In tailed bacteriophages, the portal system is connected to a tail structure that provides the pipeline for genome delivery to the host cell. We report the first, to our knowledge, subnanometer structures of the complete portal-phage tail interface that mimic the states before and after DNA release during phage infection. They uncover structural rearrangements associated with intimate protein-DNA interactions. The portal protein gp6 of bacteriophage SPP1 undergoes a concerted reorganization of the structural elements of its central channel during interaction with DNA. A network of protein-protein interactions primes consecutive binding of proteins gp15 and gp16 to extend and close the channel. This critical step that prevents genome leakage from the capsid is achieved by a previously unidentified allosteric mechanism: gp16 binding to two different regions of gp15 drives correct positioning and folding of an inner gp16 loop to interact with equivalent loops of the other gp16 subunits. Together, these loops build a plug that closes the channel. Gp16 then fastens the tail to yield the infectious virion. The gatekeeper system opens for viral genome exit at the beginning of infection but recloses afterward, suggesting a molecular diaphragm-like mechanism to control DNA efflux. The mechanisms described here, controlling the essential steps of phage genome movements during virus assembly and infection, are likely to be conserved among long-tailed phages, the largest group of viruses in the Biosphere.DNA gatekeeper | viral infection | bacteriophage | allosteric mechanism | hybrid methods

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confidence: 99%

Structural rearrangements in the phage head-to-tail interface during assembly and infection

Chaban

Lurz

Brasilès

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…In the 3D (H)CANH spectrum, the NH pair of Ala78 is correlated with its intraresidual 13 Ca resonance (red). Navigating to the determined 1 H, 15 Nand 13 Ca resonances in the 4D (H)COCANH spectrum yields the intraresidual 13 CO resonance(green). Navigating to the same resonances in the 4D (H)CBCANHspectrum yields the 13 Cb chemicalshift (blue).…”

Section: Zuschriftenmentioning

confidence: 99%

“…Hexameric rings are stacked on top of each other and rotated relative to each other by 218 8. zation of the monomeric subunit. [15] Due to the large size of gp17.1 (177 residues) and the previous restriction of solidstate NMR to 13 C-detected methods,afull chemical-shift assignment could not be obtained. Therefore,w es et out to study gp17.1 by high-dimensional 1 H-detected solid-state NMR.…”

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confidence: 99%

“…The phage tail is required for DNArelease into the host cell. [14,15] Ap reliminary analysis of gp17.1 by solid-state NMR showed that the b-sheet content increases upon polymeri- Figure 1. The tail-tube protein gp17.1 of bacteriophageS PP1.…”

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confidence: 99%

“…Our recombinant tubes are thus indistinguishable by EM from native tubes in the context of fully assembled phages. [15] Solid-state NMR experiments were conducted at 40 kHz MAS in a1.9 mm rotor at an external magnetic field strength of 900 MHz. Figure 2s hows the "fingerprint" 2D (H)NH spectrum with indicated linewidths for an isolated resonance.…”

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Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR

et al. 2017

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Obtaining unambiguous resonance assignments remains am ajor bottlenecki ns olid-state NMR studies of protein structure and dynamics.P articularly for supramolecular assemblies with large subunits (> 150 residues), the analysis of crowded spectral data presents ac hallenge,e ven if three-dimensional (3D) spectra are used. Here,w ep resent ap roton-detected 4D solid-state NMR assignment procedure that is tailored for large assemblies.T he key to recording 4D spectra with three indirect carbon or nitrogen dimensions with their inherently large chemical shift dispersion lies in the use of sparse non-uniform sampling (as lowa s2%). As ap roof of principle,weacquired 4D (H)COCANH, (H)CACONH, and (H)CBCANHs pectra of the 20 kDa bacteriophage tail-tube protein gp17.1 in at otal time of two and ah alf weeks.T hese spectra were sufficient to obtain complete resonance assignments in as traightforwardm anner without use of previous solution NMR data.

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Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR

et al. 2017

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Obtaining unambiguous resonance assignments remains a major bottleneck in solid‐state NMR studies of protein structure and dynamics. Particularly for supramolecular assemblies with large subunits (>150 residues), the analysis of crowded spectral data presents a challenge, even if three‐dimensional (3D) spectra are used. Here, we present a proton‐detected 4D solid‐state NMR assignment procedure that is tailored for large assemblies. The key to recording 4D spectra with three indirect carbon or nitrogen dimensions with their inherently large chemical shift dispersion lies in the use of sparse non‐uniform sampling (as low as 2 %). As a proof of principle, we acquired 4D (H)COCANH, (H)CACONH, and (H)CBCANH spectra of the 20 kDa bacteriophage tail‐tube protein gp17.1 in a total time of two and a half weeks. These spectra were sufficient to obtain complete resonance assignments in a straightforward manner without use of previous solution NMR data.

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Bacteriophage SPP1 Tail Tube Protein Self-assembles into β-Structure-rich Tubes

Cited by 28 publications

References 41 publications

Structural rearrangements in the phage head-to-tail interface during assembly and infection

Structural rearrangements in the phage head-to-tail interface during assembly and infection

Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR

Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR

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