Abstract
ATP-activated DNA polymerase III holoenzyme (holoenzyme) forms a stable initiation complex with primed DNA with concomitant hydrolysis of the ATP (Burgers, P. M. J., and Kornberg, A. (1982) J. Biol. Chem. 257, 11468-11478). Upon replication of primed single-stranded circular DNA to a duplex circle with a small gap (RFII), the holoenzyme remains stably bound. Dissociation requires binding by ATP or the generally nonhydrolyzable analog, adenosine 5'-(3-thiotriphosphate). Transfer of holoenzyme to another primed DNA absolutely requires ATP (or dATP) and takes about 2 min at 30 degrees C. The rate of cycling of holoenzyme is only slightly dependent on the concentration of primed DNA. However, the transfer time is reduced to only 2 to 5 s when it is intramolecular, as shown by movement to other primers on the same template chain. A rapid transfer of holoenzyme from a completed chain to another primer on the same template molecule is anticipated from the frequency of initiating nascent chains at the replicating fork of the cellular chromosome (about 1 per s at 37 degrees C) and the low cellular abundance of holoenzyme (about 10 to 20 molecules per cell).
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