## Abstract DNA polymerases which duplicate cellular chromosomes are multiprotein complexes. The individual functions of the many proteins required to duplicate a chromosome are not fully understood. The multiprotein complex which duplicates the __Escherichia coli__ chromosome, DNA polymerase III h
Assembly and disassembly of DNA polymerase holoenzyme
โ Scribed by Daniel J Sexton; Anthony J Berdis; Stephen J Benkovic
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 754 KB
- Volume
- 1
- Category
- Article
- ISSN
- 1367-5931
No coin nor oath required. For personal study only.
โฆ Synopsis
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.
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