Assembly and disassembly of DNA polymerase holoenzyme.
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.
152 Davey Laboratory, Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.
D J
DJ
Sexton
A J
AJ
Berdis
S J
SJ
Benkovic
D017122:Bacteriophage T4 / Q000201:enzymology; D003067:Coenzymes / Q000378:metabolism*; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D003067:Coenzymes; D004259:DNA-Directed DNA Polymerase