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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.

Authors:
 [1]; ORCiD logo [2];  [2];  [1];  [1];  [1];  [3];  [4];  [1]; ORCiD logo [2]
  1. Key Laboratory of Science and Technology of Eco-Textiles, Ministry of Education, College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, Shanghai 201620, China
  2. Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA
  3. National Center for Protein Science Shanghai, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201204, China
  4. Department of Diagnostic and Biological Sciences, and Institute for Molecular Virology, University of Minnesota, Minneapolis, MN 55455, USA
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
FOREIGN
OSTI Identifier:
1569887
Resource Type:
Journal Article
Journal Name:
Nucleic Acids Research
Additional Journal Information:
Journal Volume: 47; Journal Issue: 18; Journal ID: ISSN 0305-1048
Publisher:
Oxford University Press
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Cai, Rujie, Price, Ian R., Ding, Fang, Wu, Feifei, Chen, Ting, Zhang, Yunlong, Liu, Guangfeng, Jardine, Paul J., Lu, Changrui, and Ke, Ailong. ATP/ADP modulates gp16–pRNA conformational change in the Phi29 DNA packaging motor. United States: N. p., 2019. Web. doi:10.1093/nar/gkz692.
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. United States. doi:10.1093/nar/gkz692.
Cai, Rujie, Price, Ian R., Ding, Fang, Wu, Feifei, Chen, Ting, Zhang, Yunlong, Liu, Guangfeng, Jardine, Paul J., Lu, Changrui, and Ke, Ailong. Fri . "ATP/ADP modulates gp16–pRNA conformational change in the Phi29 DNA packaging motor". United States. doi:10.1093/nar/gkz692.
@article{osti_1569887,
title = {ATP/ADP modulates gp16–pRNA conformational change in the Phi29 DNA packaging motor},
author = {Cai, Rujie and Price, Ian R. and Ding, Fang and Wu, Feifei and Chen, Ting and Zhang, Yunlong and Liu, Guangfeng and Jardine, Paul J. and Lu, Changrui and Ke, Ailong},
abstractNote = {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.},
doi = {10.1093/nar/gkz692},
journal = {Nucleic Acids Research},
issn = {0305-1048},
number = 18,
volume = 47,
place = {United States},
year = {2019},
month = {8}
}