||Bacteria Escherichia coli
||Kelman Z, O'Donnell M. DNA polymerase III holoenzyme: structure and function of a chromosomal replicating machine. Annu Rev Biochem. 1995 64:171-200 p.173 3rd paragraphPubMed ID7574479
|| Studwell PS, O'Donnell M. Processive replication is contingent on the exonuclease subunit of DNA polymerase III holoenzyme. J Biol Chem. 1990 Jan 15 265(2):1171-8PubMed ID2153103
||Primary source abstract: "In this report [investigators] have taken the reconstitution approach to study which subunits of the heterotrimer core polymerase (alpha, epsilon, theta) participate in the highly processive replication of long DNA templates by DNA polymerase III holoenzyme (holoenzyme). Comparison of the core and the alpha epsilon complex (the DNA polymerase and 3'-5' exonuclease subunits, respectively) shows they are both rapid and highly processive polymerases when they are reconstituted into a holoenzyme with the gamma complex (gamma delta delta' chi psi) and beta accessory proteins of holoenzyme."
||P.173 3rd paragraph: "For example, holoenzyme was found to be exceedingly rapid in DNA synthesis-approximately 750 nucleotides/s consistent with the observed rate of fork movement in E. coli (primary source) and much faster than the 10-20 nucleotides/s of Pol I (ref 35). This rapid rate results from the high processivity of holoenzyme, which extends a chain for several thousand nucleotides without dissociating from the template even once (refs 36, 37)." See BNID 103995