Molecular assessment of S1 endonuclease-resistant snapback hairpin loops generated by DNA polymerase I during the in-vitro nick translation reaction

1985 ◽  
Vol 11 (1) ◽  
pp. 1-15
Author(s):  
Michael V. Norgard
Keyword(s):  
Dna Polymerase ◽  
Nick Translation ◽  
Dna Polymerase I ◽  
Hairpin Loops ◽  
Molecular Assessment ◽  
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.

DNA polymerase I proofreading exonuclease activity is required for endonuclease V repair pathway both in vitro and in vivo

DNA Repair ◽  
2018 ◽  
Vol 64 ◽  
pp. 59-67 ◽  
Author(s):  
Kang-Yi Su ◽  
Liang-In Lin ◽  
Steven D. Goodman ◽  
Rong-Syuan Yen ◽  
Cho-Yuan Wu ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Exonuclease Activity ◽  
Repair Pathway ◽  
Dna Polymerase I ◽  
Endonuclease V ◽  
Polymerase I

Mechanism of initiation of in vitro DNA synthesis by the immunopurified complex between yeast DNA polymerase I and DNA primase

1986 ◽  
Vol 161 (2) ◽  
pp. 435-440 ◽  
Author(s):  
Gianfranco BADARACCO ◽  
Paola VALSASNINI ◽  
Marco FOIANI ◽  
Roberta BENFANTE ◽  
Giovanna LUCCHINI ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerase ◽  
Dna Polymerase I ◽  
Dna Primase ◽  
Polymerase I

Chlamydial DNA polymerase I can bypass lesions in vitro

2006 ◽  
Vol 345 (3) ◽  
pp. 1083-1091 ◽  
Author(s):  
Xipeng Liu ◽  
Jingli Hou ◽  
Jianhua Liu
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase I ◽  
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

scholarly journals Characterization of the mitochondrial DNA polymerase from Saccharomyces cerevisiae.

1994 ◽  
Vol 41 (1) ◽  
pp. 79-86 ◽  
Author(s):  
S Sen ◽  
S Mukhopadhyay ◽  
J Wetzel ◽  
T K Biswas
Keyword(s):  
Mitochondrial Dna ◽  
Dna Polymerase ◽  
Nuclear Dna ◽  
Dna Polymerase I ◽  
Specificity And Sensitivity ◽  
Protease Deficient ◽  
Polymerase I ◽  
Mitochondrial Dna Polymerase

The mitochondrial DNA (mtDNA) polymerase was isolated from a protease-deficient yeast strain (PY2), and purified about 3000 fold by a column chromatography on phosphocellulose, heparin-agarose, and single-stranded DNA cellulose. The purified polymerase was characterized with respect to optimal nucleotide concentrations, template-primer specificity and sensitivity to some inhibitors. These results were compared with the nuclear DNA polymerase I activity. Both polymerases showed similar requirement of deoxynucleotide concentrations (Km < 1 microM), and highest activity with poly(dA-dT) template. However, the mtDNA polymerase was more sensitive to ddTTP, EtBr and Mn2+ inhibition in comparison to the nuclear DNA polymerase I. The mtDNA polymerase did not need ATP as an energy source for in vitro DNA synthesis. This mtDNA polymerase preparation also showed 3'-->5' exonuclease activity.

scholarly journals The effect of nitrofurantoin on deoxyribonucleic acid synthesis in plant mitochondria

1980 ◽  
Vol 186 (1) ◽  
pp. 325-329 ◽  
Author(s):  
S Palit ◽  
B B Goswami ◽  
D K Dube
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerase ◽  
Plant Mitochondria ◽  
Acid Synthesis ◽  
Dna Polymerase I ◽  
Avian Myeloblastosis Virus ◽  
Deoxyribonucleic Acid Synthesis ◽  
Etiolated Seedlings ◽  
Polymerase I

Nitrofurantoin (1-([(5-nitrofuran-2-yl)methylene]amino)imidazolidine-2,4-dione), a widely used drug and also a well-known bacterial mutagen, inhibits DNA synthesis in mitochondria from 48 h etiolated seedlings of Vigna sinensis (Linn.) Savi (snake bean). The effect appears at the level of the uptake of radioactive deoxynucleoside triphosphates by the plant mitochondria. Nitrofurantoin does not inhibit DNA synthesis in vitro by homogeneous Escherichia coli DNA polymerase I and DNA polymerase from avian-myeloblastosis virus. No specific nitroreductase activity could be detected in mitochondria.

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