Fine structure and assembly pattern of a minimal myophage Pam3

Author:

Yang Feng12,Jiang Yong-Liang1,Zhang Jun-Tao1,Zhu Jie1ORCID,Du Kang1,Yu Rong-Cheng1,Wei Zi-Lu1,Kong Wen-Wen1ORCID,Cui Ning1,Li Wei-Fang1,Chen Yuxing1ORCID,Li Qiong1ORCID,Zhou Cong-Zhao1

Affiliation:

1. School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230026, China

2. Research Center for Intelligent Computing Platforms, Zhejiang Lab, Hangzhou, Zhejiang 311121, China

Abstract

The myophage possesses a contractile tail that penetrates its host cell envelope. Except for investigations on the bacteriophage T4 with a rather complicated structure, the assembly pattern and tail contraction mechanism of myophage remain largely unknown. Here, we present the fine structure of a freshwater Myoviridae cyanophage Pam3, which has an icosahedral capsid of ~680 Å in diameter, connected via a three-section neck to an 840-Å-long contractile tail, ending with a three-module baseplate composed of only six protein components. This simplified baseplate consists of a central hub-spike surrounded by six wedge heterotriplexes, to which twelve tail fibers are covalently attached via disulfide bonds in alternating upward and downward configurations. In vitro reduction assays revealed a putative redox-dependent mechanism of baseplate assembly and tail sheath contraction. These findings establish a minimal myophage that might become a user-friendly chassis phage in synthetic biology.

Funder

Ministry of Science and Technology of the People's Republic of China

National Natural Science Foundation of China

Strategic Priority Strategic Priority Research Program of the Chinese Academy of Sciences

Youth Innovation Promotion Association of Chinese Academy of Sciences

the Fundamental Research Funds for the Central Universities

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

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