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DNA polymerase III delta subunit, C-terminal domain
Processivity clamp loader gamma complex DNA pol III C-term
This domain lies at the C-terminus of the delta subunit of the DNA polymerase III clamp loader gamma complex. Within the complex the several C-terminal domains, of gamma, delta and delta' form a helical scaffold, on which the rest of he subunits are hung. The gamma complex, an AAA+ ATPase, is the bacterial homologue of the eukaryotic replication factor C that loads the sliding clamp (beta, homologous to PCNA) onto DNA. [1]. 11525729. Crystal structure of the processivity clamp loader gamma (gamma). complex of E. coli DNA polymerase III.. Jeruzalmi D, O'Donnell M, Kuriyan J;. Cell. 2001;106:429-441. (from Pfam)
DNA polymerase III, delta subunit
DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalysed reaction [1]. The delta subunit is also known as HolA. [1]. 11432857. The delta and delta ' subunits of the DNA polymerase III. holoenzyme are essential for initiation complex formation and. processive elongation.. Song MS, Pham PT, Olson M, Carter JR, Franden MA, Schaaper RM,. McHenry CS;. J Biol Chem 2001;276:35165-35175. (from Pfam)
DNA polymerase III subunit delta
DNA polymerase III delta (holA) and delta-prime (holB) subunits are distinct proteins encoded by separate genes. The delta, delta-prime, gamma, chi and psi subunits form the gamma complex subassembly of DNA polymerase III holoenzyme, which couples ATP to assemble the ring-shaped beta subunit around DNA forming a DNA sliding clamp.
DNA polymerase III subunit delta interacts with the delta' and gamma subunits and is part of the clamp-loading complex, which assembles the beta processivity factor onto the primer template, plays a central role in the organization and communication at the replication fork and present in initiation complex which is required for processive elongation.
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