A Smaller Form of the Sliding Clamp Subunit of DNA Polymerase III Is Induced by UV Irradiation in Escherichia coli

Autor: Tamar Paz-Elizur, Rami Skaliter, Zvi Livneh
Rok vydání: 1996
Předmět:
Zdroj: Journal of Biological Chemistry. 271:2478-2481
ISSN: 0021-9258
DOI: 10.1074/jbc.271.5.2478
Popis: The beta subunit of DNA polymerase III holoenzyme of Escherichia coli is a 40.6-kDa protein that functions as a sliding DNA clamp (Stukenberg, P. T., Studwell-Vaughan, P. S., and O'Donnell, M. (1991) J. Biol. Chem. 266, 11328-11334). It is responsible for tethering the polymerase to DNA and endowing it with the high processivity required for DNA replication. Here and in a companion study (Paz-Elizur, T., Skaliter, R., Blumenstein, S., and Livneh, Z. (1996) J. Biol. Chem. 271, 2482-2490) we report that the dnaN gene, encoding the beta subunit, contains an internal in-frame gene, termed dnaN*, that encodes a smaller form of the beta subunit. The novel 26-kDa protein, termed beta*, is UV-inducible, and when overexpressed from a plasmid under an inducible promoter, it increases up to 6-fold the UV resistance of E. coli cells. These findings suggest that the beta* protein functions in a reaction associated with DNA repair or recovery of DNA replication in UV-irradiated cells.
Databáze: OpenAIRE