Document Type
Article
Publication Date
10-1-1997
Publication Title
Current Opinion in Chemical Biology
Abstract
The complex task of genomic replication requires a large collection of proteins properly assembled within the close confines of the replication fork. The mechanism and dynamics of holoenzyme assembly and disassembly have been investigated using steady state and pre-steady state methods as opposed to structural studies, primarily due to the intrinsic transient nature of these protein complexes during DNA replication. The key step in bacteriophage T4 holoenzyme assembly involves ATP hydrolysis, whereas disassembly is mediated by subunit dissociation of the clamp protein in an ATP-independent manner.
Recommended Citation
Sexton, Daniel J.; Berdis, Anthony J.; and Benkovic, Stephen J., "Assembly and Disassembly of DNA Polymerase Holoenzyme" (1997). Chemistry Faculty Publications. 171.
https://engagedscholarship.csuohio.edu/scichem_facpub/171
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
DOI
10.1016/S1367-5931(97)80068-3
Version
Postprint
Volume
1
Issue
3
