Tail Structure and Dynamics

Bhatt, Shweta; Leiman, P.G.; Taylor, Nicholas M. I.

doi:10.1016/b978-0-12-809633-8.20965-5

Cited by 1 publication

(1 citation statement)

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“…These flexibly tethered tail fibers of Pam3 should increase the searching space for the host receptors and thereby promoting the capability of Pam3 to recognize and infect the host. Once Pam3 baseplate approaches the cell surface, a signaling cascade is triggered to drive the sheath contraction in a way similar to other myophages and CISs ( 11 , 30 , 31 ). For Pam3, redox signaling should play a role in reorienting the wedge heterotriplexes and eventually initiating sheath contraction.…”

Section: Discussionmentioning

confidence: 99%

Fine structure and assembly pattern of a minimal myophage Pam3

Yang

Jiang

Zhang

et al. 2023

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

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The myophage possesses a contractile tail that penetrates its host cell envelope. Except for investigations on the bacteriophage T4 with a rather complicated structure, the assembly pattern and tail contraction mechanism of myophage remain largely unknown. Here, we present the fine structure of a freshwater Myoviridae cyanophage Pam3, which has an icosahedral capsid of ~680 Å in diameter, connected via a three-section neck to an 840-Å-long contractile tail, ending with a three-module baseplate composed of only six protein components. This simplified baseplate consists of a central hub-spike surrounded by six wedge heterotriplexes, to which twelve tail fibers are covalently attached via disulfide bonds in alternating upward and downward configurations. In vitro reduction assays revealed a putative redox-dependent mechanism of baseplate assembly and tail sheath contraction. These findings establish a minimal myophage that might become a user-friendly chassis phage in synthetic biology.

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Section: Discussionmentioning

confidence: 99%