ArticleStructure (London, England : 1993)2013
Structure of the PolIIIα-τc-DNA complex suggests an atomic model of the replisome.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Pre-Steady-State Kinetic Characterization of an Antibiotic-Resistant Mutant of Staphylococcus aureus DNA Polymerase PolC.Antimicrobial agents and chemotherapy · 2023Article
- Interactions of small molecules with DNA junctions.Nucleic acids research · 2022Review
- Error-prone DnaE2 Balances the Genome Mutation Rates inFrontiers in microbiology · 2017Article
- cryo-EM structures of theeLife · 2015Article
- DNA Polymerase α Subunit Residues and Interactions Required for Efficient Initiation Complex Formation Identified by a Genetic Selection.The Journal of biological chemistry · 2015Article
- Helicase and polymerase move together close to the fork junction and copy DNA in one-nucleotide steps.Cell reports · 2014Article
- Cycling of the E. coli lagging strand polymerase is triggered exclusively by the availability of a new primer at the replication fork.Nucleic acids research · 2014Article
- Comprehensive analysis of DNA polymerase III α subunits and their homologs in bacterial genomes.Nucleic acids research · 2014Article
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3 authors.
Funding
Abstract
The C-terminal domain (CTD) of the τ subunit of the clamp loader (τc) binds to both the DnaB helicase and the DNA polymerase III α subunit (PolIIIα), and determines their relative positions and orientations on the leading and lagging strands. Here, we present a 3.2 Å resolution structure of Thermus aquaticus PolIIIα in complex with τc and a DNA substrate. The structure reveals that the CTD of τc interacts with the CTD of PolIIIα through its C-terminal helix and the adjacent loop. Additionally, in this complex PolIIIα displays an open conformation that includes the reorientations of the oligonucleotide-binding fold and the thumb domain, which may be an indirect result of crystal packing due to the presence of the τc. Nevertheless, the position of the τc on PolIIIα allows us to suggest an approximate model for how the PolIIIα is oriented and positioned on the DnaB helicase.
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