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DNA polymerase III clamp loader subunit, ATPase lid domain
This entry represents the AAA+ ATPase lid domain of DNA polymerase III clamp loader subunit [1-4]. Paper describing PDB structure 1jr3. [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. Paper describing PDB structure 1njf. [2]. 12623013. Nucleotide-induced conformational changes in an isolated Escherichia coli DNA polymerase III clamp loader subunit. Podobnik M, Weitze TF, O'Donnell M, Kuriyan J;. Structure. 2003;11:253-263. Paper describing PDB structure 1xxi. [3]. 15556993. Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex. Kazmirski SL, Podobnik M, Weitze TF, O'Donnell M, Kuriyan J;. Proc Natl Acad Sci U S A. 2004;101:16750-16755. Paper describing PDB structure 3glf. [4]. 19450514. The mechanism of ATP-dependent primer-template recognition by a clamp loader complex. Simonetta KR, Kazmirski SL, Goedken ER, Cantor AJ, Kelch BA, McNally R, Seyedin SN, Makino DL, O'Donnell M, Kuriyan J;. Cell. 2009;137:659-671. (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 subunits gamma and tau domain III
This domain family is found in bacteria, and is approximately 110 amino acids in length. The family is found in association with Pfam:PF00004. Domains I-III are shared between the tau and the gamma subunits, while most of the DnaB-binding Domain IV and all of the alpha-interacting Domain V are unique to tau. [1]. 17355988. The unstructured C-terminus of the tau subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the alpha subunit. Jergic S, Ozawa K, Williams NK, Su XC, Scott DD, Hamdan SM, Crowther JA, Otting G, Dixon NE;. Nucleic Acids Res. 2007;35:2813-2824. (from Pfam)
Holliday junction DNA helicase RuvB P-loop domain
The RuvB protein makes up part of the RuvABC revolvasome which catalyses the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalysed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein [1]. This family contains the N-terminal region of the protein. [1]. 12423347. The RuvABC resolvasome. Dickman MJ, Ingleston SM, Sedelnikova SE, Rafferty JB, Lloyd RG, Grasby JA, Hornby DP;. Eur J Biochem 2002;269:5492-5501. (from Pfam)
AAA family ATPase
AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2]. [1]. 7646486. A 200-amino acid ATPase module in search of a basic function. Confalonieri F, Duguet M;. Bioessays 1995;17:639-650. A large extension of the family. [2]. 9927482. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Neuwald AF, Aravind L, Spouge JL, Koonin EV;. Genome Res 1999;9:27-43. (from Pfam)
DNA polymerase III subunit gamma/tau
DNA polymerase III subunit gamma/tau is part of the DNA polymerase III holoenzyme; gamma and tau subunits are isoforms and either one or both may be present in the holoenzyme; gamma interacts with the delta subunit to transfer the beta subunit on the DNA while tau serves as a scaffold to help in the dimerization of the core complex
This model represents the well-conserved first ~ 365 amino acids of the translation of the dnaX gene. The full-length product of the dnaX gene in the model bacterium E. coli is the DNA polymerase III tau subunit. A translational frameshift leads to early termination and a truncated protein subunit gamma, about 1/3 shorter than tau and present in roughly equal amounts. This frameshift mechanism is not necessarily universal for species with DNA polymerase III but appears conserved in the exterme thermophile Thermus thermophilis.
Catalyzes the DNA-template-directed extension of the 3'-end of a DNA strand; the tau chain serves as a scaffold to help in the dimerizaton of the alpha,epsilon and theta core complex; the gamma chain seems to interact with the delta and delta' subunits to transfer the beta subunit on the DNA
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