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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 DOI Help

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

Open Access Open Access

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)