Isolation, sequencing and overexpression of the gene encoding theθsubunit of DNA polymerase III holoenzyme
- 11 July 1993
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 21 (14) , 3281-3286
- https://doi.org/10.1093/nar/21.14.3281
Abstract
The gene encoding the θ subunit of DNA polymerase III hoioenzyme, designated holE, was isolated using a strategy in which peptide sequence was used to derive a DNA hybridization probe. Sequencing of the gene, which maps to 41.43 centisomes of the chromosome, revealed a 76-codon open reading frame predicted to produce a protein of 8,846 Da. When piaced in a tac promoter expression vector, the open reading frame directed expression of a protein, that comigrated with authentic θ subunit from purified hoioenzyme, to 6% of total soluble protein.Keywords
This publication has 47 references indexed in Scilit:
- DNA polymerase III holoenzyme of Escherichia coli. II. A novel complex including the gamma subunit essential for processive synthesis.Published by Elsevier ,2021
- Molecular cloning and DNA sequence analysis of Escherichia coli priA, the gene encoding the primosomal protein replication factor Y.Proceedings of the National Academy of Sciences, 1990
- Alignment of Escherichia coli K12 DNA sequences to a genomic restriction mapNucleic Acids Research, 1990
- Processive replication is contingent on the exonuclease subunit of DNA polymerase III holoenzyme.Journal of Biological Chemistry, 1990
- DNA POLYMERASE III HOLOENZYME OF ESCHERICHIA COLIAnnual Review of Biochemistry, 1988
- The primosomal protein n' of Escherichia coli is a DNA helicase.Journal of Biological Chemistry, 1988
- Improved tools for biological sequence comparison.Proceedings of the National Academy of Sciences, 1988
- Accessory proteins bind a primed template and mediate rapid cycling of DNA polymerase III holoenzyme from Escherichia coli.Journal of Biological Chemistry, 1987
- Escherichia coli replication factor Y, a component of the primosome, can act as a DNA helicase.Proceedings of the National Academy of Sciences, 1987
- The Escherichia coli preprimosome and DNA B helicase can form replication forks that move at the same rate.Journal of Biological Chemistry, 1987