Correction: In vitro Bypass of UV-induced lesions by Escherichia coli DNA Polymerase I: Specificity of Nucleotide Incorporation

1983 ◽  
Vol 80 (12) ◽  
pp. 3870-3870
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Dna Polymerase I ◽  
Nucleotide Incorporation ◽  
Polymerase I

Caffeine inhibits DNA polymerase I from Escherichia coli: studies in vitro

1982 ◽  
Vol 3 (2) ◽  
pp. 151-153 ◽  
Author(s):  
R. Balachandran ◽  
A. Srinivasan
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Dna Polymerase I ◽  
Polymerase I

Viroid RNA is accepted as a template for in vitro transcription by DNA-dependent DNA polymerase I and RNA polymerase from Escherichia coli

1982 ◽  
Vol 2 (11) ◽  
pp. 929-939 ◽  
Author(s):  
Wolfgang Rohde ◽  
Hans-Richard Rackwitz ◽  
Frank Boege ◽  
Heinz L. Sänger
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Dna Polymerase ◽  
Unit Length ◽  
Dna Polymerase I ◽  
Experimental Conditions ◽  
In Vitro Synthesis ◽  
Polymerase I

The RNA genome of potato spindle tuber viroid (PSTV) is transcribed in vitro into complementary DNA and RNA by DNA-dependent DNA polymerase I and RNA polymerase, respectively, from Escherichia coli. In vitro synthesis of complementary RNA produces distinct transcripts larger than unit length thus reflecting the in vivo mechanism of viroid replication. The influence of varying experimental conditions on the transcription process is studied; actinomycin D is found to drastically reduce complementary RNA synthesis from the PSTV RNA template by RNA polymerase.

scholarly journals Assessment of the genotoxic potential of nitric oxide-induced guanine lesions by in vitro reactions with Escherichia coli DNA polymerase I

Mutagenesis ◽  
2005 ◽  
Vol 20 (3) ◽  
pp. 209-216 ◽  
Author(s):  
Toshiaki Nakano ◽  
Kenjiro Asagoshi ◽  
Hiroaki Terato ◽  
Toshinori Suzuki ◽  
Hiroshi Ide
Keyword(s):  
Nitric Oxide ◽  
Escherichia Coli ◽  
Dna Polymerase ◽  
Dna Polymerase I ◽  
Genotoxic Potential ◽  
Polymerase I

scholarly journals Escherichia coli β-clamp slows down DNA polymerase I dependent nick translation while accelerating ligation

2018 ◽  
Author(s):  
Amit Bhardwaj ◽  
Debarghya Ghose ◽  
Krishan Gopal Thakur ◽  
Dipak Dutta
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Nick Translation ◽  
Dna Polymerase I ◽  
Okazaki Fragments ◽  
Pol I ◽  
Dna Strands ◽  
Translation Property ◽  
Polymerase I

AbstractThe nick translation property of DNA polymerase I (Pol I) ensures the maturation of Okazaki fragments by removing primer RNAs and facilitating ligation. However, prolonged nick translation traversing downstream DNA is an energy wasting futile process, as Pol I simultaneously polymerizes and depolymerizes at the nick sites utilizing energy-rich dNTPs. Using an in vitro assay system, we demonstrate that the β-clamp of the Escherichia coli replisome strongly inhibits nick translation on the DNA substrate. To do so, β-clamp inhibits the strand displacement activity of Pol I by interfering with the interaction between the finger subdomain of Pol I and the downstream primer-template junction. Conversely, β-clamp stimulates the 5’ exonuclease property of Pol I to cleave single nucleotides or shorter oligonucleotide flaps. This single nucleotide flap removal at high frequency increases the probability of ligation between the upstream and downstream DNA strands at an early phase, terminating nick translation. Besides β-clamp-mediated ligation helps DNA ligase to seal the nick promptly during the maturation of Okazaki fragments.

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