DNA Polymerase III Holoenzyme of Escherichia Coli: An Asymmetric Dimeric Replicative Complex Containing Distinguishable Leading and Lagging Strand Polymerases
- 1 January 1984
- book chapter
- Published by Springer Nature
- Vol. 179, 315-319
- https://doi.org/10.1007/978-1-4684-8730-5_32
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- The beta subunit of the DNA polymerase III holoenzyme becomes inaccessible to antibody after formation of an initiation complex with primed DNA.Journal of Biological Chemistry, 1982
- ATP activation of DNA polymerase III holoenzyme of Escherichia coli. I. ATP-dependent formation of an initiation complex with a primed template.Journal of Biological Chemistry, 1982
- ATP activation of DNA polymerase III holoenzyme from Escherichia coli. II. Initiation complex: stoichiometry and reactivity.Journal of Biological Chemistry, 1982
- Purification and characterization of DNA polymerase III'. Identification of tau as a subunit of the DNA polymerase III holoenzyme.Journal of Biological Chemistry, 1982
- Purification and characterization of the beta subunit of the DNA polymerase III holoenzyme of Escherichia coli.Journal of Biological Chemistry, 1980
- Efficient in vitro replication of double-stranded DNA templates by a purified T4 bacteriophage replication system.Journal of Biological Chemistry, 1980
- DNA polymerase III of Escherichia coli. Purification and identification of subunits.Journal of Biological Chemistry, 1979
- DNA polymerase III holoenzyme of Escherichia coli. Purification and resolution into subunits.Journal of Biological Chemistry, 1977
- Mechanism of DNA elongation catalyzed by Escherichia coli DNA polymerase III, dnaZ protein, and DNA elongation factors I and III.Proceedings of the National Academy of Sciences, 1976
- DNA Polymerase III Star Requires ATP to Start Synthesis on a Primed DNAProceedings of the National Academy of Sciences, 1973