FIGURE 4 | Architecture of the replicative DNA polymerase III holoenzyme from E. coli.

From the following article:

The 3'–5' exonucleases

Igor V. Shevelev & Ulrich Hübscher

Nature Reviews Molecular Cell Biology 3, 364-376 (May 2002)

doi:10.1038/nrm804

The 3|[prime]||[ndash]|5|[prime]| exonucleases

The DNA polymerase III holoenzyme is a multisubunit complex, which consists of 17 polypeptides. It contains four subassemblies. First, the core polymerase consists of three subunits: alpha (the polymerase); alt epsilon (the 3'–5' exonuclease); and theta (the stimulator of the 3'–5' exonuclease). Second, the tau subunit is responsible for dimerization of the core DNA polymerase. Third, the sliding clamp comprises two homodimers of the beta subunit, which provides the ring structure that is needed for processivity. Fourth, five subunits have clamp-loader functions — gamma, delta, delta', chi and psi. For details, see Ref. 34.

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