The Phage T4 Antiholin RI Has a Cleavable Signal Peptide, Not a SAR Domain

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Mehner-Breitfeld, D.; Schwarzkopf, J.M.F.; Young, R.; Kondabagil, K.; Brüser, T.: The Phage T4 Antiholin RI Has a Cleavable Signal Peptide, Not a SAR Domain. In: Frontiers in Microbiology 12 (2021), 712460. DOI:

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Sum total of downloads: 55

Holin/endolysin-mediated lysis of phage T4 of Escherichia coli is tightly regulated by the antiholins RI and RIII. While regulation by the cytoplasmic RIII plays a minor role, the periplasmic antiholin RI binds tightly to the holin T and is believed to directly sense periplasmic phage DNA from superinfections as a trigger for the inhibition of lysis. RI has been reported to contain a non-cleavable signal peptide that anchors the protein to the membrane. Lysis is believed to be induced at some stage by a membrane depolarization that causes a release of RI into the periplasm without cleavage of the signal anchor. For the current model of phage lysis induction, it is thus a fundamental assumption that the N-terminal trans-membrane domain (TMD) of RI is such a signal anchor release (SAR) domain. Here we show that, in contrast to previous reports, this domain of RI is a cleavable signal peptide. RI is processed and released into the periplasm as a mature protein, and inactivation of its signal peptidase cleavage site blocks processing and membrane release. The signal peptide of RI can also mediate the normal translocation of a well-characterized Sec substrate, PhoA, into the periplasm. This simplifies the current view of phage lysis regulation and suggests a fundamentally different interpretation of the recently published structure of the soluble domains of the RI-T complex.
License of this version: CC BY 4.0 Unported
Document Type: Article
Publishing status: publishedVersion
Issue Date: 2021
Appears in Collections:Naturwissenschaftliche Fakultät

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4 image of flag of France France 3 5.45%
5 image of flag of Russian Federation Russian Federation 2 3.64%
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