Topological examination of the bacteriophage lambda S holin by EPR spectroscopy.
Bacteriophage lysis
EPR spectroscopy
Pore-forming protein
Journal
Biochimica et biophysica acta. Biomembranes
ISSN: 1879-2642
Titre abrégé: Biochim Biophys Acta Biomembr
Pays: Netherlands
ID NLM: 101731713
Informations de publication
Date de publication:
02 2023
02 2023
Historique:
received:
01
04
2022
revised:
26
10
2022
accepted:
31
10
2022
pmc-release:
01
02
2024
pubmed:
13
11
2022
medline:
21
12
2022
entrez:
12
11
2022
Statut:
ppublish
Résumé
The S protein from bacteriophage lambda is a three-helix transmembrane protein produced by the prophage which accumulates in the host membrane during late gene expression. It is responsible for the first step in lysing the host cell at the end of the viral life cycle by multimerizing together to form large pores which permeabilize the host membrane to allow the escape of virions. Several previous studies have established a model for the assembly of holin into functional holes and the manner in which they pack together, but it is still not fully understood how the very rapid transition from monomer or dimer to multimeric pore occurs with such precise timing once the requisite threshold is reached. Here, site-directed spin labeling with a nitroxide label at introduced cysteine residues is used to corroborate existing topological data from a crosslinking study of the multimerized holin by EPR spectroscopy. CW-EPR spectral lineshape analysis and power saturation data are consistent with a three-helix topology with an unstructured C-terminal domain, as well as at least one interface on transmembrane domain 1 which is exposed to the lumen of the hole, and a highly constrained steric environment suggestive of a tight helical packing interface at transmembrane domain 2.
Identifiants
pubmed: 36370910
pii: S0005-2736(22)00221-8
doi: 10.1016/j.bbamem.2022.184083
pmc: PMC9771973
mid: NIHMS1850555
pii:
doi:
Substances chimiques
Cysteine
K848JZ4886
Membrane Proteins
0
Spin Labels
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
184083Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM126935
Pays : United States
Informations de copyright
Copyright © 2022 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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