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

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 moto...

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Autores principales: Cai, Rujie, Price, Ian R, Ding, Fang, Wu, Feifei, Chen, Ting, Zhang, Yunlong, Liu, Guangfeng, Jardine, Paul J, Lu, Changrui, Ke, Ailong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2019
Materias:
RNA and RNA-protein complexes
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6765105/
https://www.ncbi.nlm.nih.gov/pubmed/31396619
http://dx.doi.org/10.1093/nar/gkz692
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author Cai, Rujie
Price, Ian R
Ding, Fang
Wu, Feifei
Chen, Ting
Zhang, Yunlong
Liu, Guangfeng
Jardine, Paul J
Lu, Changrui
Ke, Ailong
author_facet Cai, Rujie
Price, Ian R
Ding, Fang
Wu, Feifei
Chen, Ting
Zhang, Yunlong
Liu, Guangfeng
Jardine, Paul J
Lu, Changrui
Ke, Ailong
author_sort Cai, Rujie
collection PubMed
description 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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spelling pubmed-67651052019-10-02 ATP/ADP modulates gp16–pRNA conformational change in the Phi29 DNA packaging motor Cai, Rujie Price, Ian R Ding, Fang Wu, Feifei Chen, Ting Zhang, Yunlong Liu, Guangfeng Jardine, Paul J Lu, Changrui Ke, Ailong Nucleic Acids Res RNA and RNA-protein complexes 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. Oxford University Press 2019-10-10 2019-08-09 /pmc/articles/PMC6765105/ /pubmed/31396619 http://dx.doi.org/10.1093/nar/gkz692 Text en © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle RNA and RNA-protein complexes
Cai, Rujie
Price, Ian R
Ding, Fang
Wu, Feifei
Chen, Ting
Zhang, Yunlong
Liu, Guangfeng
Jardine, Paul J
Lu, Changrui
Ke, Ailong
ATP/ADP modulates gp16–pRNA conformational change in the Phi29 DNA packaging motor
title ATP/ADP modulates gp16–pRNA conformational change in the Phi29 DNA packaging motor
title_full ATP/ADP modulates gp16–pRNA conformational change in the Phi29 DNA packaging motor
title_fullStr ATP/ADP modulates gp16–pRNA conformational change in the Phi29 DNA packaging motor
title_full_unstemmed ATP/ADP modulates gp16–pRNA conformational change in the Phi29 DNA packaging motor
title_short ATP/ADP modulates gp16–pRNA conformational change in the Phi29 DNA packaging motor
title_sort atp/adp modulates gp16–prna conformational change in the phi29 dna packaging motor
topic RNA and RNA-protein complexes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6765105/
https://www.ncbi.nlm.nih.gov/pubmed/31396619
http://dx.doi.org/10.1093/nar/gkz692
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