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Structural studies reveal a ring-shaped architecture of deep-sea vent phage NrS-1 polymerase
NrS-1 is the first known phage that can infect Epsilonproteobacteria, one of the predominant primary producers in the deep-sea hydrothermal vent ecosystems. NrS-1 polymerase is a multidomain enzyme and is one key component of the phage replisome. The N-terminal Prim/Pol and HBD domains are responsib...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7102993/ https://www.ncbi.nlm.nih.gov/pubmed/32016421 http://dx.doi.org/10.1093/nar/gkaa071 |
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author | Chen, Xi Su, Shichen Chen, Yiqing Gao, Yanqing Li, Yangyang Shao, Zhiwei Zhang, Yixi Shao, Qiyuan Liu, Hehua Li, Jixi Ma, Jinbiao Gan, Jianhua |
author_facet | Chen, Xi Su, Shichen Chen, Yiqing Gao, Yanqing Li, Yangyang Shao, Zhiwei Zhang, Yixi Shao, Qiyuan Liu, Hehua Li, Jixi Ma, Jinbiao Gan, Jianhua |
author_sort | Chen, Xi |
collection | PubMed |
description | NrS-1 is the first known phage that can infect Epsilonproteobacteria, one of the predominant primary producers in the deep-sea hydrothermal vent ecosystems. NrS-1 polymerase is a multidomain enzyme and is one key component of the phage replisome. The N-terminal Prim/Pol and HBD domains are responsible for DNA polymerization and de novo primer synthesis activities of NrS-1 polymerase. However, the structure and function of the C-terminus (CTR) of NrS-1 polymerase are poorly understood. Here, we report two crystal structures, showing that NrS-1 CTR adopts one unique hexameric ring-shaped conformation. Although the central helicase domain of NrS-1 CTR shares structural similarity with the superfamily III helicases, the folds of the Head and Tail domains are completely novel. Via mutagenesis and in vitro biochemical analysis, we identified many residues important for the helicase and polymerization activities of NrS-1 polymerase. In addition to NrS-1 polymerase, our study may also help us identify and understand the functions of multidomain polymerases expressed by many NrS-1 related phages. |
format | Online Article Text |
id | pubmed-7102993 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-71029932020-04-02 Structural studies reveal a ring-shaped architecture of deep-sea vent phage NrS-1 polymerase Chen, Xi Su, Shichen Chen, Yiqing Gao, Yanqing Li, Yangyang Shao, Zhiwei Zhang, Yixi Shao, Qiyuan Liu, Hehua Li, Jixi Ma, Jinbiao Gan, Jianhua Nucleic Acids Res Structural Biology NrS-1 is the first known phage that can infect Epsilonproteobacteria, one of the predominant primary producers in the deep-sea hydrothermal vent ecosystems. NrS-1 polymerase is a multidomain enzyme and is one key component of the phage replisome. The N-terminal Prim/Pol and HBD domains are responsible for DNA polymerization and de novo primer synthesis activities of NrS-1 polymerase. However, the structure and function of the C-terminus (CTR) of NrS-1 polymerase are poorly understood. Here, we report two crystal structures, showing that NrS-1 CTR adopts one unique hexameric ring-shaped conformation. Although the central helicase domain of NrS-1 CTR shares structural similarity with the superfamily III helicases, the folds of the Head and Tail domains are completely novel. Via mutagenesis and in vitro biochemical analysis, we identified many residues important for the helicase and polymerization activities of NrS-1 polymerase. In addition to NrS-1 polymerase, our study may also help us identify and understand the functions of multidomain polymerases expressed by many NrS-1 related phages. Oxford University Press 2020-04-06 2020-02-04 /pmc/articles/PMC7102993/ /pubmed/32016421 http://dx.doi.org/10.1093/nar/gkaa071 Text en © The Author(s) 2020. 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 | Structural Biology Chen, Xi Su, Shichen Chen, Yiqing Gao, Yanqing Li, Yangyang Shao, Zhiwei Zhang, Yixi Shao, Qiyuan Liu, Hehua Li, Jixi Ma, Jinbiao Gan, Jianhua Structural studies reveal a ring-shaped architecture of deep-sea vent phage NrS-1 polymerase |
title | Structural studies reveal a ring-shaped architecture of deep-sea vent phage NrS-1 polymerase |
title_full | Structural studies reveal a ring-shaped architecture of deep-sea vent phage NrS-1 polymerase |
title_fullStr | Structural studies reveal a ring-shaped architecture of deep-sea vent phage NrS-1 polymerase |
title_full_unstemmed | Structural studies reveal a ring-shaped architecture of deep-sea vent phage NrS-1 polymerase |
title_short | Structural studies reveal a ring-shaped architecture of deep-sea vent phage NrS-1 polymerase |
title_sort | structural studies reveal a ring-shaped architecture of deep-sea vent phage nrs-1 polymerase |
topic | Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7102993/ https://www.ncbi.nlm.nih.gov/pubmed/32016421 http://dx.doi.org/10.1093/nar/gkaa071 |
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