The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria

Aksyuk, Anastasia A.; Leiman, P.G.; Kurochkina, Lidia P.; Shneider, Mikhail M.; Kostyuchenko, V.A.; Mesyanzhinov, Vadim V.; Rossmann, Michael G.

doi:10.1038/emboj.2009.36

Cited by 142 publications

(177 citation statements)

References 38 publications

Supporting

Mentioning

171

Contrasting

Order By: Relevance

“…4C). However, isolated tail sheath proteins of T4 and other Myoviridae phages spontaneously assemble into so-called "polysheaths" that resemble contracted tail sheaths in their subunit organization (27,28,30,31). Therefore, the structure of the native phi812 tail provides experimental proof of a previous speculation that assembly of the metastable Myoviridae tail sheaths is determined by tail tube protein-tail sheath protein interactions (32).…”

Section: Significancesupporting

confidence: 50%

“…The individual disks are stacked into a six-entry helix with a pitch of 38.9 Å and twist of 21.4°. Despite the lower than 15% sequence identity between the T4, phiKZ, and phi812 tail sheath proteins, the four domains constituting the proteins have similar structures (27,28). However, the relative positions of the domains within the tail sheath proteins of the phages differ (SI Appendix, Fig.…”

Section: Significancementioning

confidence: 99%

“…Thus, domain I is required to hold domain II in position so that it can form interactions within the tail sheath protein hexamer. In contrast, domains I and II of the T4 tail sheath protein are located parallel to each other with a limited contact interface, and domain I was proposed to be dispensable for tail sheath formation (13,18,28,29). Domain III of the phi812 tail sheath protein interacts with domain IV from a tail sheath protein positioned toward the baseplate (Fig.…”

Section: Significancementioning

confidence: 99%

See 2 more Smart Citations

Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate

Nováček

Šiborová

Benešík

et al. 2016

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

View full text Add to dashboard Cite

Bacteriophages from the family Myoviridae use double-layered contractile tails to infect bacteria. Contraction of the tail sheath enables the tail tube to penetrate through the bacterial cell wall and serve as a channel for the transport of the phage genome into the cytoplasm. However, the mechanisms controlling the tail contraction and genome release of phages with “double-layered” baseplates were unknown. We used cryo-electron microscopy to show that the binding of the Twort-like phage phi812 to the Staphylococcus aureus cell wall requires a 210° rotation of the heterohexameric receptor-binding and tripod protein complexes within its baseplate about an axis perpendicular to the sixfold axis of the tail. This rotation reorients the receptor-binding proteins to point away from the phage head, and also results in disruption of the interaction of the tripod proteins with the tail sheath, hence triggering its contraction. However, the tail sheath contraction of Myoviridae phages is not sufficient to induce genome ejection. We show that the end of the phi812 double-stranded DNA genome is bound to one protein subunit from a connector complex that also forms an interface between the phage head and tail. The tail sheath contraction induces conformational changes of the neck and connector that result in disruption of the DNA binding. The genome penetrates into the neck, but is stopped at a bottleneck before the tail tube. A subsequent structural change of the tail tube induced by its interaction with the S. aureus cell is required for the genome’s release.

show abstract

Section: Significancesupporting

confidence: 50%

Section: Significancementioning

confidence: 99%

Section: Significancementioning

confidence: 99%

See 1 more Smart Citation

Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate

Nováček

Šiborová

Benešík

et al. 2016

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

View full text Add to dashboard Cite

show abstract

“…4 The contractile sheath structure The bacteriophage T4 tail is the most extensively studied contractile system. 128,129,137,146,147 The structure of the T4 tail before and after contraction has been determined using cryo-EM ( Fig. 14A and B).…”

Section: Structure Of the Phage Tailsmentioning

confidence: 99%

Molecular architecture of tailed double-stranded DNA phages

2014

Self Cite

View full text Add to dashboard Cite

“…It is surmised that there must be another step, perhaps the head joining, which makes the extended tail sheath highly stable against dissociation. The crystal structure of gp18 was later solved by Aksyuk et al (2009).…”

Section: Ph-dependent Reversible Association Of Gp5 and Gp27mentioning

confidence: 99%

Protein interactions in the assembly of the tail of bacteriophage T4

Arisaka

Kanamaru

2013

Biophys Rev

View full text Add to dashboard Cite

Protein interactions in the assembly of the baseplate have been investigated. The baseplate of the phage T4 tail consists of a hub and six wedges which surround the former. Both reversible and irreversible interactions were found. Reversible association includes gp5 and gp27 (gp: gene product) which form a complex in a pH-dependent manner and gp18 polymerization, i.e. the tail sheath formation depends on the ionic strength. These reversible interactions were followed by irreversible or tight binding which pulls the whole association reaction to complete the assembly. The wedge assembly is strictly ordered which means that if one of the seven wedge proteins is missing, the assembly proceeds to that point and the remaining molecules stay non-associated. The strictly sequential assembly pathway is suggested to be materialized by successive conformational change upon binding, which can be shown by proteolytic probe.

show abstract

The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria

Cited by 142 publications

References 38 publications

Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate

Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate

Molecular architecture of tailed double-stranded DNA phages

Protein interactions in the assembly of the tail of bacteriophage T4

Contact Info

Product

Resources

About