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Insights into the mechanism of action of the arbitrium communication system in SPbeta phages
DOI:
10.1038/s41467-022-31144-3
Authors:
Francisca
Gallego Del Sol
(Instituto de Biomedicina de Valencia (IBV-CSIC); CIBER de Enfermedades Raras (CIBERER))
,
Nuria
Quiles-Puchalt
(Imperial College London)
,
Aisling
Brady
(Imperial College London; University of Glasgow)
,
José R.
Penadés
(Imperial College London)
,
Alberto
Marina
(Instituto de Biomedicina de Valencia (IBV), CSIC and CIBER de Enfermedades Raras (CIBERER))
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Nature Communications
, VOL 13
State:
Published (Approved)
Published:
June 2022
Diamond Proposal Number(s):
28394

Abstract: The arbitrium system is employed by phages of the SPbeta family to communicate with their progeny during infection to decide either to follow the lytic or the lysogenic cycle. The system is controlled by a peptide, AimP, that binds to the regulator AimR, inhibiting its DNA-binding activity and expression of aimX. Although the structure of AimR has been elucidated for phages SPβ and phi3T, there is still controversy regarding the molecular mechanism of AimR function, with two different proposed models for SPβ. In this study, we deepen our understanding of the system by solving the structure of an additional AimR that shows chimerical characteristics with the SPβ receptor. The crystal structures of this AimR (apo, AimP-bound and DNA-bound) together with in vitro and in vivo analyses confirm a mechanism of action by AimP-induced conformational restriction, shedding light on peptide specificity and cross regulation with relevant biological implications.
Diamond Keywords: Bacteriophages; Viruses
Subject Areas:
Biology and Bio-materials
Instruments:
I24-Microfocus Macromolecular Crystallography
Other Facilities: XALOC at ALBA; ID23-2 at ESRF
Added On:
29/06/2022 09:24
Documents:
s41467-022-31144-3.pdf
Discipline Tags:
Structural biology
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)