dc.identifier.uri |
http://dx.doi.org/10.15488/11750 |
|
dc.identifier.uri |
https://www.repo.uni-hannover.de/handle/123456789/11843 |
|
dc.contributor.author |
Mehner-Breitfeld, Denise
|
|
dc.contributor.author |
Schwarzkopf, Jan Michel Frederik
|
|
dc.contributor.author |
Young, Ry
|
|
dc.contributor.author |
Kondabagil, Kiran
|
|
dc.contributor.author |
Brüser, Thomas
|
|
dc.date.accessioned |
2022-02-01T09:31:05Z |
|
dc.date.available |
2022-02-01T09:31:05Z |
|
dc.date.issued |
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: https://doi.org/10.3389/fmicb.2021.712460 |
|
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) |
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dc.rights |
CC BY 4.0 Unported |
|
dc.rights.uri |
https://creativecommons.org/licenses/by/4.0/ |
|
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.relation.doi |
https://doi.org/10.3389/fmicb.2021.712460 |
|
dc.bibliographicCitation.volume |
12 |
|
dc.bibliographicCitation.firstPage |
712460 |
|
dc.description.version |
publishedVersion |
|
tib.accessRights |
frei zug�nglich |
|