Spanish Ministry of Science, Innovation, and Universities
BFU 2014-54181
Spain
Spanish Ministry of Science, Innovation, and Universities
SEV-2013-0347
Spain
Spanish Ministry of Science, Innovation, and Universities
BES-2015-073615
Spain
Citation
Journal: Proc Natl Acad Sci U S A / Year: 2021 Title: Assisted assembly of bacteriophage T7 core components for genome translocation across the bacterial envelope. Authors: Mar Pérez-Ruiz / Mar Pulido-Cid / Juan Román Luque-Ortega / José María Valpuesta / Ana Cuervo / José L Carrascosa / Abstract: In most bacteriophages, genome transport across bacterial envelopes is carried out by the tail machinery. In viruses of the family, in which the tail is not long enough to traverse the bacterial ...In most bacteriophages, genome transport across bacterial envelopes is carried out by the tail machinery. In viruses of the family, in which the tail is not long enough to traverse the bacterial wall, it has been postulated that viral core proteins assembled inside the viral head are translocated and reassembled into a tube within the periplasm that extends the tail channel. Bacteriophage T7 infects , and despite extensive studies, the precise mechanism by which its genome is translocated remains unknown. Using cryo-electron microscopy, we have resolved the structure of two different assemblies of the T7 DNA translocation complex composed of the core proteins gp15 and gp16. Gp15 alone forms a partially folded hexamer, which is further assembled upon interaction with gp16 into a tubular structure, forming a channel that could allow DNA passage. The structure of the gp15-gp16 complex also shows the location within gp16 of a canonical transglycosylase motif involved in the degradation of the bacterial peptidoglycan layer. This complex docks well in the tail extension structure found in the periplasm of T7-infected bacteria and matches the sixfold symmetry of the phage tail. In such cases, gp15 and gp16 that are initially present in the T7 capsid eightfold-symmetric core would change their oligomeric state upon reassembly in the periplasm. Altogether, these results allow us to propose a model for the assembly of the core translocation complex in the periplasm, which furthers understanding of the molecular mechanism involved in the release of T7 viral DNA into the bacterial cytoplasm.
A: Internal virion protein gp15 B: Internal virion protein gp15 C: Internal virion protein gp15 D: Internal virion protein gp15 E: Internal virion protein gp15 F: Internal virion protein gp15
Average exposure time: 35 sec. / Electron dose: 30 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 2470
Image scans
Movie frames/image: 32
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Processing
EM software
ID
Name
Category
1
Gautomatch
particleselection
2
EPU
imageacquisition
4
CTFFIND
CTFcorrection
7
Coot
modelfitting
9
PHENIX
modelrefinement
10
RELION
initialEulerassignment
11
RELION
finalEulerassignment
12
RELION
classification
13
RELION
3Dreconstruction
CTF correction
Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Symmetry
Point symmetry: C6 (6 fold cyclic)
3D reconstruction
Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 50980 / Algorithm: FOURIER SPACE / Num. of class averages: 1 / Symmetry type: POINT
Atomic model building
Protocol: AB INITIO MODEL / Space: REAL
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