ArticleNucleic acids research2007
The unstructured C-terminus of the tau subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the alpha subunit.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 60 citations in OpenAlex.
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- Escherichia coli DNA replication: the old model organism still holds many surprises.FEMS microbiology reviews · 2024Review
- The Escherichia coli clamp loader rapidly remodels SSB on DNA to load clamps.Nucleic acids research · 2022Article
- DnaB helicase dynamics in bacterial DNA replication resolved by single-molecule studies.Nucleic acids research · 2021Article
- Novel Antibiotics Targeting Bacterial Replicative DNA Polymerases.Antibiotics (Basel, Switzerland) · 2020Review
- A Primase-Induced Conformational Switch Controls the Stability of the Bacterial Replisome.Molecular cell · 2020Article
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- Genome-Wide Identification and Expression, Protein-Protein Interaction and Evolutionary Analysis of the Seed Plant-SpecificFrontiers in plant science · 2017Article
- The β2 clamp in the Mycobacterium tuberculosis DNA polymerase III αβ2ε replicase promotes polymerization and reduces exonuclease activity.Scientific reports · 2016Article
- cryo-EM structures of theeLife · 2015Article
- Plasmid replication initiator interactions with origin 13-mers and polymerase subunits contribute to strand-specific replisome assembly.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Polymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III α binding to ssDNA.Nucleic acids research · 2013Article
- A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode.The EMBO journal · 2013Article
- Bacterial replication, transcription and translation: mechanistic insights from single-molecule biochemical studies.Nature reviews. Microbiology · 2013Review
- Structure of the PolIIIα-τc-DNA complex suggests an atomic model of the replisome.Structure (London, England : 1993) · 2013Article
- Selective disruption of the DNA polymerase III α-β complex by the umuD gene products.Nucleic acids research · 2012Article
- Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.Current drug targets · 2012Review
- Investigating the predictability of essential genes across distantly related organisms using an integrative approach.Nucleic acids research · 2011Article
- dnaX36 Mutator of Escherichia coli: effects of the {tau} subunit of the DNA polymerase III holoenzyme on chromosomal DNA replication fidelity.Journal of bacteriology · 2011Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tau subunit of Escherichia coli DNA polymerase III holoenzyme interacts with the alpha subunit through its C-terminal Domain V, tau(C)16. We show that the extreme C-terminal region of tau(C)16 constitutes the site of interaction with alpha. The tau(C)16 domain, but not a derivative of it with a C-terminal deletion of seven residues (tau(C)16Delta7), forms an isolable complex with alpha. Surface plasmon resonance measurements were used to determine the dissociation constant (K(D)) of the alpha-tau(C)16 complex to be approximately 260 pM. Competition with immobilized tau(C)16 by tau(C)16 derivatives for binding to alpha gave values of K(D) of 7 muM for the alpha-tau(C)16Delta7 complex. Low-level expression of the genes encoding tau(C)16 and tau(C)16triangle up7, but not tau(C)16Delta11, is lethal to E. coli. Suppression of this lethal phenotype enabled selection of mutations in the 3' end of the tau(C)16 gene, that led to defects in alpha binding. The data suggest that the unstructured C-terminus of tau becomes folded into a helix-loop-helix in its complex with alpha. An N-terminally extended construct, tau(C)24, was found to bind DNA in a salt-sensitive manner while no binding was observed for tau(C)16, suggesting that the processivity switch of the replisome functionally involves Domain IV of tau.
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