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Get a quoteWebClamp loaders perform the mechanical task of opening clamps and depositing them on DNA templates ( 3 ). The binding and hydrolysis of ATP drive this assembly reaction. The E. coli clamp loader is composed of five different subunits, three copies of the dnaX gene product (γ and/or τ), δ, δ′, χ, and ψ ( 4, 5, 6, 7 ).
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Get a quoteWebClamp loaders perform the mechanical task of opening clamps and depositing them on DNA templates ( 3 ). The binding and hydrolysis of ATP drive this assembly reaction. The E. coli clamp loader is composed of five different subunits, three copies of the dnaX gene product (γ and/or τ), δ, δ′, χ, and ψ ( 4, 5, 6, 7 ).
Get a quoteWebClamp loader of Escherichia coli DNA Polymerase III : kinetics of the ATP-dependent steps in the sliding-clamp loading reaction Item Preview
Get a quoteWebAug 18, 2015 · Solution study of the Escherichia coli DNA polymerase III clamp loader reveals the location of the dynamic ψχ heterodimer Structural Dynamics 2, 054701 (2015); https://doi.org/10.1063/1.4927407 Farzaneh Tondnevis 1, Richard E. Gillilan 2, Linda B. Bloom 1, and Robert McKenna 1, a) View Affiliations View Contributors PDF CHORUS …
Get a quoteWebJul 5, 2011 · Escherichia coli DNA polymerase III is a highly processive replicase due to the presence of the β clamp protein that tethers DNA polymerases to DNA. The β clamp is a head-to-tail ring-shaped homodimer, in which each protomer contains three structurally similar domains.
Get a quoteWebThe Escherichia coliDNA polymerase III gamma complex clamp loader assembles the ring-shaped beta sliding clamp onto DNA. The core polymerase is tethered to the template by beta, enabling progressive replication of the genome. The E. coli complex clamp loader contains five different subunits, clamp loading only requires 3 of these - the gamma
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Get a quoteWebFeb 12, 2022 · This result confirms that a clamp loader complex deficient of HolD also induces the SOS response in P. aeruginosa. Figure 3 HolD depletion induces the SOS response and affects the expression of DNA polymerases.
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