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

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dc.identifier.uri Mehner-Breitfeld, Denise Schwarzkopf, Jan Michel Frederik Young, Ry Kondabagil, Kiran Brüser, Thomas 2022-02-01T09:31:05Z 2022-02-01T09:31:05Z 2021
dc.identifier.citation 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:
dc.description.abstract 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. eng
dc.language.iso eng
dc.publisher Lausanne : Frontiers Media
dc.relation.ispartofseries Frontiers in Microbiology 12 (2021)
dc.rights CC BY 4.0 Unported
dc.subject phage lysis eng
dc.subject holins eng
dc.subject antiholins eng
dc.subject lysis inhibition eng
dc.subject signal peptide eng
dc.subject SAR domain eng
dc.subject.ddc 570 | Biowissenschaften, Biologie ger
dc.title The Phage T4 Antiholin RI Has a Cleavable Signal Peptide, Not a SAR Domain
dc.type Article
dc.type Text
dc.relation.essn 1664-302X
dc.bibliographicCitation.volume 12
dc.bibliographicCitation.firstPage 712460
dc.description.version publishedVersion
tib.accessRights frei zug�nglich

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