ArticleNucleic acids research2004
Genome wide, supercoiling-dependent in vivo binding of a viral protein involved in DNA replication and transcriptional control.
Article in Nucleic acids research, 2004. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Flexible structural arrangement and DNA-binding properties of protein p6 from Bacillus subtillis phage φ29.Nucleic acids research · 2024Article
- DNA-Binding Proteins Essential for Protein-Primed Bacteriophage Φ29 DNA Replication.Frontiers in molecular biosciences · 2016Review
- Disclosing the in vivo organization of a viral histone-like protein in Bacillus subtilis mediated by its capacity to recognize the viral genome.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- In vivo DNA binding of bacteriophage GA-1 protein p6.Journal of bacteriology · 2007Article
- The phage phi29 membrane protein p16.7, involved in DNA replication, is required for efficient ejection of the viral genome.Journal of bacteriology · 2007Article
- Phage phi29 proteins p1 and p17 are required for efficient binding of architectural protein p6 to viral DNA in vivo.Journal of bacteriology · 2004Article
- Binding of phage Phi29 architectural protein p6 to the viral genome: evidence for topological restriction of the phage linear DNA.Nucleic acids research · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein p6 of Bacillus subtilis bacteriophage Phi29 is essential for phage development. In vitro it activates the initiation of DNA replication and is involved in the early to late transcriptional switch. These activities require the formation of a nucleoprotein complex in which the DNA forms a right-handed superhelix wrapping around a multimeric protein core. However, there was no evidence of p6 binding to Phi29 DNA in vivo. By crosslinking, chromatin immunoprecipitation and real-time PCR we show that protein p6 binds to most, if not all, the viral genome in vivo, although with higher affinity for both DNA ends, which contain the replication origins. In contrast, the affinity for plasmid DNA is negligible, but greatly increases when the negative supercoiling decreases, as shown in vivo by treatment of cells with novobiocin and in vitro by fluorescence quenching with plasmids with different topology. In conclusion, binding of protein p6 all along the Phi29 genome strongly suggests that its functions in replication and transcription control could be local outcomes of a more global role as a histone-like protein. The p6 binding dependence on DNA topology could explain its preferential binding to viral with respect to bacterial DNA, whose level of negative supercoiling is presumably higher than that of Phi29 DNA.
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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.