ArticleNucleic acids research2014
Intrinsic stability and oligomerization dynamics of DNA processivity clamps.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Responses to Ligand Binding in the Bacterial DNA Sliding Clamp "β-Clamp" Manifest in Dynamic Allosteric Effects.Proteins · 2025Article
- Long-Range Destabilizing Effects of Mutations at theBiochemistry · 2025Article
- Functional asymmetry in processivity clamp proteins.Biophysical journal · 2025Review
- Structural characterisation of the complete cycle of sliding clamp loading in Escherichia coli.Nature communications · 2024Article
- Escherichia coli DNA replication: the old model organism still holds many surprises.FEMS microbiology reviews · 2024Review
- The bacterial DNA sliding clamp, β-clamp: structure, interactions, dynamics and drug discovery.Cellular and molecular life sciences : CMLS · 2024Review
- Review
- Article
- Potassium Glutamate and Glycine Betaine Induce Self-Assembly of the PCNA and β-Sliding Clamps.Biophysical journal · 2021Article
- Dynamics of the E. coli β-Clamp Dimer Interface and Its Influence on DNA Loading.Biophysical journal · 2019Article
- Recognition of a Key Anchor Residue by a Conserved Hydrophobic Pocket Ensures Subunit Interface Integrity in DNA Clamps.Journal of molecular biology · 2019Article
- Mechanism of opening a sliding clamp.Nucleic acids research · 2017Article
- Electrostatic Interactions at the Dimer Interface Stabilize the E. coli β Sliding Clamp.Biophysical journal · 2017Article
- Dynamics of Open DNA Sliding Clamps.PloS one · 2016Article
- The assembly dynamics of the cytolytic pore toxin ClyA.Nature communications · 2015Article
- Kinetic analysis of PCNA clamp binding and release in the clamp loading reaction catalyzed by Saccharomyces cerevisiae replication factor C.Biochimica et biophysica acta · 2015Article
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Authors and funding
7 authors.
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Abstract
Sliding clamps are ring-shaped oligomeric proteins that are essential for processive deoxyribonucleic acid replication. Although crystallographic structures of several clamps have been determined, much less is known about clamp structure and dynamics in solution. Here, we characterized the intrinsic solution stability and oligomerization dynamics of the homodimeric Escherichia coli β and the homotrimeric Saccharomyces cerevisiae proliferating cell nuclear antigen (PCNA) clamps using single-molecule approaches. We show that E. coli β is stable in solution as a closed ring at concentrations three orders of magnitude lower than PCNA. The trimeric structure of PCNA results in slow subunit association rates and is largely responsible for the lower solution stability. Despite this large difference, the intrinsic lifetimes of the rings differ by only one order of magnitude. Our results show that the longer lifetime of the E. coli β dimer is due to more prominent electrostatic interactions that stabilize the subunit interfaces.
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