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 | |
| Publication status | Published - Aug 1 1995 |
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All Science Journal Classification (ASJC) codes
- Microbiology
- Molecular Biology
- Genetics
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Isolation and characterization of inhibitory factors of DNA polymerase III holoenzyme from Escherichia coli. / Hase, Masakazu; Mizushima, Tohru; Katayama, Tsutomu; Sekimizu, Kazuhisa.
In: FEMS microbiology letters, Vol. 130, No. 2-3, 01.08.1995, p. 215-220.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Isolation and characterization of inhibitory factors of DNA polymerase III holoenzyme from Escherichia coli
AU - Hase, Masakazu
AU - Mizushima, Tohru
AU - Katayama, Tsutomu
AU - Sekimizu, Kazuhisa
PY - 1995/8/1
Y1 - 1995/8/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0029100278&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029100278&partnerID=8YFLogxK
U2 - 10.1016/0378-1097(95)00209-N
DO - 10.1016/0378-1097(95)00209-N
M3 - Article
VL - 130
SP - 215
EP - 220
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
SN - 0378-1097
IS - 2-3
ER -