ArticleNucleic acids research2012
A flexible brace maintains the assembly of a hexameric replicative helicase during DNA unwinding.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- Assembly of a homohexameric minichromosome maintenance complex is dependent on ATP and DNA.The Journal of biological chemistry · 2026Article
- Unwinding of a DNA replication fork by a hexameric viral helicase.Nature communications · 2021Article
- Requirement for the E1 Helicase C-Terminal Domain in Papillomavirus DNA Replication In Vivo.Journal of virology · 2016Article
- Structural basis for DNA strand separation by a hexameric replicative helicase.Nucleic acids research · 2015Article
- A conserved regulatory module at the C terminus of the papillomavirus E1 helicase domain controls E1 helicase assembly.Journal of virology · 2015Article
- Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea.Nature communications · 2014Article
- Dynamic look at DNA unwinding by a replicative helicase.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The E1 proteins.Virology · 2013Review
- Characterization of an unusual bipolar helicase encoded by bacteriophage T5.Nucleic acids research · 2013Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The mechanism of DNA translocation by papillomavirus E1 and polyomavirus LTag hexameric helicases involves consecutive remodelling of subunit-subunit interactions around the hexameric ring. Our biochemical analysis of E1 helicase demonstrates that a 26-residue C-terminal segment is critical for maintaining the hexameric assembly. As this segment was not resolved in previous crystallographic analysis of E1 and LTag hexameric helicases, we determined the solution structure of the intact hexameric E1 helicase by Small Angle X-ray Scattering. We find that the C-terminal segment is flexible and occupies a cleft between adjacent subunits in the ring. Electrostatic potential calculations indicate that the negatively charged C-terminus can bridge the positive electrostatic potentials of adjacent subunits. Our observations support a model in which the C-terminal peptide serves as a flexible 'brace' maintaining the oligomeric state during conformational changes associated with ATP hydrolysis. We argue that these interactions impart processivity to DNA unwinding. Sequence and disorder analysis suggest that this mechanism of hexamer stabilization would be conserved among papillomavirus E1 and polyomavirus LTag hexameric helicases.
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Registered trials
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