ArticleNucleic acids research2020
Structural studies reveal a ring-shaped architecture of deep-sea vent phage NrS-1 polymerase.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 14 citations in OpenAlex.
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- Structural and functional insights into the helicase protein E5 of Mpox virus.Cell discovery · 2024Article
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- Structures and implications of the C962R protein of African swine fever virus.Nucleic acids research · 2023Article
- Functional biology and biotechnology of thermophilic viruses.Essays in biochemistry · 2023Review
- The Vaccinia Virus DNA Helicase Structure from Combined Single-Particle Cryo-Electron Microscopy and AlphaFold2 Prediction.Viruses · 2022Article
- Staphylococcal self-loading helicases couple the staircase mechanism with inter domain high flexibility.Nucleic acids research · 2022Article
- Bacteriophage-Encoded DNA Polymerases-Beyond the Traditional View of Polymerase Activities.International journal of molecular sciences · 2022Review
- Molecular Dissection of the Primase and Polymerase Activities of Deep-Sea Phage NrS-1 Primase-Polymerase.Frontiers in microbiology · 2021Article
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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