ArticleViruses2021
A Structural Perspective of Reps from CRESS-DNA Viruses and Their Bacterial Plasmid Homologues.
Article in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Identification of novel CRESS-DNA viruses in the human vaginal microbiome.Frontiers in microbiology · 2026Article
- Trans-replicase helper activity of porcine circoviruses promotes the synergistic replication of torque teno virus.Frontiers in microbiology · 2024Article
- Genomic analysis of hyperparasitic viruses associated with entomopoxviruses.Virus evolution · 2024Article
- Phylogenomic analysis expands the known repertoire of single-stranded DNA viruses in benthic zones of the South Indian Ocean.ISME communications · 2024Article
- Molecular characterization of a tetra segmented ssDNA virus infecting Botrytis cinerea worldwide.Virology journal · 2023Article
- Article
- Deciphering the Origin of DNA Viruses (Replication-Associated Parvo-NS1) That Infect Vertebrates from Invertebrate-Infecting Viruses.Microbiology spectrum · 2023Article
- Replitrons: A major group of eukaryotic transposons encoding HUH endonuclease.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Evolution of anelloviruses from a circovirus-like ancestor through gradual augmentation of the jelly-roll capsid protein.Virus evolution · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Rolling circle replication (RCR) is ubiquitously used by cellular and viral systems for genome and plasmid replication. While the molecular mechanism of RCR has been described, the structural mechanism is desperately lacking. Circular-rep encoded single stranded DNA (CRESS-DNA) viruses employ a viral encoded replicase (Rep) to initiate RCR. The recently identified prokaryotic homologues of Reps may also be responsible for initiating RCR. Reps are composed of an endonuclease, oligomerization, and ATPase domain. Recent structural studies have provided structures for all these domains such that an overall mechanism of RCR initiation can begin to be synthesized. However, structures of Rep in complex with its various DNA substrates and/or ligands are lacking. Here we provide a 3D bioinformatic review of the current structural information available for Reps. We combine an excess of 1590 sequences with experimental and predicted structural data from 22 CRESS-DNA groups to identify similarities and differences between Reps that lead to potentially important functional sites. Experimental studies of these sites may shed light on how Reps execute their functions. Furthermore, we identify Rep-substrate or Rep-ligand structures that are urgently needed to better understand the structural mechanism of RCR.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.