ArticleNucleic acids research2009
DNA translocation activity of the multifunctional replication protein ORF904 from the archaeal plasmid pRN1.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- The Vaccinia Virus DNA Helicase Structure from Combined Single-Particle Cryo-Electron Microscopy and AlphaFold2 Prediction.Viruses · 2022Article
- Molecular Dissection of the Primase and Polymerase Activities of Deep-Sea Phage NrS-1 Primase-Polymerase.Frontiers in microbiology · 2021Article
- Identification of the minimal replicon and the origin of replication of the crenarchaeal plasmid pRN1.MicrobiologyOpen · 2014Article
- Functional characterization of the origin of replication of pRN1 from Sulfolobus islandicus REN1H1.PloS one · 2013Article
- The archaeo-eukaryotic primase of plasmid pRN1 requires a helix bundle domain for faithful primer synthesis.Nucleic acids research · 2010Article
- Two novel families of plasmids from hyperthermophilic archaea encoding new families of replication proteins.Nucleic acids research · 2010Article
- Merging molecular electron microscopy and mass spectrometry by carbon film-assisted endoproteinase digestion.Molecular & cellular proteomics : MCP · 2010Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The replication protein ORF904 from the plasmid pRN1 is a multifunctional enzyme with ATPase-, primase- and DNA polymerase activity. Sequence analysis suggests the presence of at least two conserved domains: an N-terminal prim/pol domain with primase and DNA polymerase activities and a C-terminal superfamily 3 helicase domain with a strong double-stranded DNA dependant ATPase activity. The exact molecular function of the helicase domain in the process of plasmid replication remains unclear. Potentially this motor protein is involved in duplex remodelling and/or origin opening at the plasmid replication origin. In support of this we found that the monomeric replication protein ORF904 forms a hexameric ring in the presence of DNA. It is able to translocate along single-stranded DNA in 3'-5' direction as well as on double-stranded DNA. Critical residues important for ATPase activity and DNA translocation activity were identified and are in agreement with a homology model of the helicase domain. In addition we propose that a winged helix DNA-binding domain at the C-terminus of the helicase domain could assist the binding of the replication protein specifically to the replication origin.
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