Insights into the mechanism of action of the arbitrium communication system in SPbeta phages.

Insights into the mechanism of action of the arbitrium communication system in SPbeta phages.
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DOI:
10.1038/s41467-022-31144-3
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发表时间:
2022-06-24
影响因子:
16.6
通讯作者:
Marina, Alberto
Marina, Alberto
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Gallego del Sol, Francisca;Quiles-Puchalt, Nuria;Brady, Aisling;Penades, Jose R.;Marina, Alberto

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在感染期间,SPbeta家族的细菌利用仲裁系统与它们的后代进行交流,以决定是遵循裂解循环还是溶原循环。该系统由一种肽AimP控制,该肽与调节剂AimR结合,抑制其DNA结合活性和aimX的表达。虽然AimR的结构已经被阐明为β-SPβ和phi 3 T,但关于AimR功能的分子机制仍然存在争议,SPβ有两种不同的模型。在这项研究中,我们通过解决一个额外的AimR的结构来加深我们对该系统的理解,该AimR与SPβ受体具有嵌合特征。该AimR的晶体结构(载脂蛋白、AimP结合和DNA结合)以及体外和体内分析证实了AimP诱导的构象限制的作用机制,揭示了肽特异性和交叉调节的相关生物学意义。Arbitrium系统是一种基于肽的通讯系统,用于协调细菌感染的裂解-溶原循环。Gallego del Sol等人在此提供了感染B的Katmira噬菌体的Aim受体的晶体结构。枯草芽孢杆菌中的载脂蛋白,肽结合和DNA结合的形式。
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. The arbitrium system is a peptide-based communication system to coordinate the lysis-lysogenic cycle of phages infecting bacteria. Here Gallego del Sol et al. provide the crystal structure of Aim-receptor of Katmira phage infecting B. subtilis in apo, peptide-bound and DNA-bound form.
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