ATP/ADP modulates gp16-pRNA conformational change in the Phi29 DNA packaging motor

Rujie Cai; Ian R. Price; Fang Ding; Feifei Wu; Ting Chen; Yunlong Zhang; Guangfeng Liu; Paul J. Jardine; Changrui Lu; Ailong Ke

doi:10.1093/nar/gkz692

ATP/ADP modulates gp16-pRNA conformational change in the Phi29 DNA packaging motor

Rujie Cai, Ian R. Price, Fang Ding, Feifei Wu, Ting Chen, Yunlong Zhang, Guangfeng Liu, Paul J. Jardine, Changrui Lu, Ailong Ke

Basic Sciences

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Abstract

Packaging of phage phi29 genome requires the ATPase gp16 and prohead RNA (pRNA). The highly conserved pRNA forms the interface between the connector complex and gp16. Understanding how pRNA interacts with gp16 under packaging conditions can shed light on the molecular mechanism of the packaging motor. Here, we present 3D models of the pRNA-gp16 complex and its conformation change in response to ATP or ADP binding. Using a combination of crystallography, small angle X-ray scattering and chemical probing, we find that the pRNA and gp16 forms a 'Z'-shaped complex, with gp16 specifically binds to pRNA domain II. The whole complex closes in the presence of ATP, and pRNA domain II rotates open as ATP hydrolyzes, before resetting after ADP is released. Our results suggest that pRNA domain II actively participates in the packaging process.

Original language	English (US)
Pages (from-to)	9818-9828
Number of pages	11
Journal	Nucleic acids research
Volume	47
Issue number	18
DOIs	https://doi.org/10.1093/nar/gkz692
State	Published - Oct 10 2019

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Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

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title = "ATP/ADP modulates gp16-pRNA conformational change in the Phi29 DNA packaging motor",

abstract = "Packaging of phage phi29 genome requires the ATPase gp16 and prohead RNA (pRNA). The highly conserved pRNA forms the interface between the connector complex and gp16. Understanding how pRNA interacts with gp16 under packaging conditions can shed light on the molecular mechanism of the packaging motor. Here, we present 3D models of the pRNA-gp16 complex and its conformation change in response to ATP or ADP binding. Using a combination of crystallography, small angle X-ray scattering and chemical probing, we find that the pRNA and gp16 forms a 'Z'-shaped complex, with gp16 specifically binds to pRNA domain II. The whole complex closes in the presence of ATP, and pRNA domain II rotates open as ATP hydrolyzes, before resetting after ADP is released. Our results suggest that pRNA domain II actively participates in the packaging process.",

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AU - Cai, Rujie

AU - Price, Ian R.

AU - Ding, Fang

AU - Wu, Feifei

AU - Chen, Ting

AU - Zhang, Yunlong

AU - Liu, Guangfeng

AU - Jardine, Paul J.

AU - Lu, Changrui

AU - Ke, Ailong

PY - 2019/10/10

Y1 - 2019/10/10

N2 - Packaging of phage phi29 genome requires the ATPase gp16 and prohead RNA (pRNA). The highly conserved pRNA forms the interface between the connector complex and gp16. Understanding how pRNA interacts with gp16 under packaging conditions can shed light on the molecular mechanism of the packaging motor. Here, we present 3D models of the pRNA-gp16 complex and its conformation change in response to ATP or ADP binding. Using a combination of crystallography, small angle X-ray scattering and chemical probing, we find that the pRNA and gp16 forms a 'Z'-shaped complex, with gp16 specifically binds to pRNA domain II. The whole complex closes in the presence of ATP, and pRNA domain II rotates open as ATP hydrolyzes, before resetting after ADP is released. Our results suggest that pRNA domain II actively participates in the packaging process.

AB - Packaging of phage phi29 genome requires the ATPase gp16 and prohead RNA (pRNA). The highly conserved pRNA forms the interface between the connector complex and gp16. Understanding how pRNA interacts with gp16 under packaging conditions can shed light on the molecular mechanism of the packaging motor. Here, we present 3D models of the pRNA-gp16 complex and its conformation change in response to ATP or ADP binding. Using a combination of crystallography, small angle X-ray scattering and chemical probing, we find that the pRNA and gp16 forms a 'Z'-shaped complex, with gp16 specifically binds to pRNA domain II. The whole complex closes in the presence of ATP, and pRNA domain II rotates open as ATP hydrolyzes, before resetting after ADP is released. Our results suggest that pRNA domain II actively participates in the packaging process.

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JO - Nucleic acids research

JF - Nucleic acids research

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ATP/ADP modulates gp16-pRNA conformational change in the Phi29 DNA packaging motor

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