Structures of Mature and Urea-Treated Empty Bacteriophage T5: Insights into Siphophage Infection and DNA Ejection

被引:6
作者
Peng, Yuning [1 ,2 ]
Tang, Huanrong [3 ]
Xiao, Hao [1 ]
Chen, Wenyuan [1 ]
Song, Jingdong [2 ]
Zheng, Jing [1 ]
Liu, Hongrong [1 ]
机构
[1] Hunan Normal Univ, Inst Interdisciplinary Studies, Key Lab Matter Microstruct & Funct Hunan Prov, Key Lab Low Dimens Quantum Struct & Quantum Contro, Changsha 410082, Peoples R China
[2] Chinese Ctr Dis Control & Prevent, Natl Inst Viral Dis Control & Prevent, Natl Key Lab Intelligent Tracking & Forecasting In, Beijing 100052, Peoples R China
[3] Xiangtan Univ, Sch Comp Sci, Xiangtan 411105, Peoples R China
基金
中国国家自然科学基金;
关键词
bacteriophage T5; siphophage; urea-treated empty particle; connector complex; cryo-EM; CRYO-EM; RESOLUTION STRUCTURE; TAIL; MICROSCOPY; PROTEINS; PARTICLES; SUGGESTS; GENOME; SHOWS; LONG;
D O I
10.3390/ijms25158479
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
T5 is a siphophage that has been extensively studied by structural and biochemical methods. However, the complete in situ structures of T5 before and after DNA ejection remain unknown. In this study, we used cryo-electron microscopy (cryo-EM) to determine the structures of mature T5 (a laboratory-adapted, fiberless T5 mutant) and urea-treated empty T5 (lacking the tip complex) at near-atomic resolutions. Atomic models of the head, connector complex, tail tube, and tail tip were built for mature T5, and atomic models of the connector complex, comprising the portal protein pb7, adaptor protein p144, and tail terminator protein p142, were built for urea-treated empty T5. Our findings revealed that the aforementioned proteins did not undergo global conformational changes before and after DNA ejection, indicating that these structural features were conserved among most myophages and siphophages. The present study elucidates the underlying mechanisms of siphophage infection and DNA ejection.
引用
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页数:14
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