Isolation and characterization of inhibitory factors of DNA polymerase III holoenzyme from Escherichia coli

Masakazu Hase; Tohru Mizushima; Tsutomu Katayama; Kazuhisa Sekimizu

doi:10.1016/0378-1097(95)00209-N

Isolation and characterization of inhibitory factors of DNA polymerase III holoenzyme from Escherichia coli

Masakazu Hase, Tohru Mizushima, Tsutomu Katayama, Kazuhisa Sekimizu

Pharmaceutical Health Care and Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

We isolated fractions by Mono Q chromatography that inhibited the activity of Escherichia coli DNA polymerase III holoenzyme using an assay system with a primed single-stranded DNA template coated with single-stranded DNA binding protein (SSB). The inhibitory activities were inactivated by heat-treatment at 100 °C for 10 min, suggesting that they are proteins. The factors did not inhibit the activity of RNA polymerase of Escherichia coli. The inhibitory effects were less potent for the activities of the large (Klenow) fragment of DNA polymerase I and T4 DNA polymerase than for DNA polymerase HI holoenzyme. No degradation of single-or double-stranded DNA was observed in the fractions, indicating that inhibition was not due to degradation of the DNA.

Original language	English
Pages (from-to)	215-220
Number of pages	6
Journal	FEMS microbiology letters
Volume	130
Issue number	2-3
DOIs	https://doi.org/10.1016/0378-1097(95)00209-N
Publication status	Published - Aug 1 1995

All Science Journal Classification (ASJC) codes

Microbiology
Molecular Biology
Genetics

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abstract = "We isolated fractions by Mono Q chromatography that inhibited the activity of Escherichia coli DNA polymerase III holoenzyme using an assay system with a primed single-stranded DNA template coated with single-stranded DNA binding protein (SSB). The inhibitory activities were inactivated by heat-treatment at 100 °C for 10 min, suggesting that they are proteins. The factors did not inhibit the activity of RNA polymerase of Escherichia coli. The inhibitory effects were less potent for the activities of the large (Klenow) fragment of DNA polymerase I and T4 DNA polymerase than for DNA polymerase HI holoenzyme. No degradation of single-or double-stranded DNA was observed in the fractions, indicating that inhibition was not due to degradation of the DNA.",

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AU - Hase, Masakazu

AU - Mizushima, Tohru

AU - Katayama, Tsutomu

AU - Sekimizu, Kazuhisa

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