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

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

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.

scholarly journals Catalytically inactive T7 DNA polymerase imposes a lethal replication roadblock

2020 ◽  
Vol 295 (28) ◽  
pp. 9542-9550
Author(s):  
Alfredo J. Hernandez ◽  
Seung-Joo Lee ◽  
Seungwoo Chang ◽  
Jaehun A. Lee ◽  
Joseph J. Loparo ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Metal Binding ◽  
Polymerase Activity ◽  
Stable Complex ◽  
Klenow Fragment ◽  
Dna Polymerase I ◽  
E Coli ◽  
Growth System ◽  
Polymerase I

Bacteriophage T7 encodes its own DNA polymerase, the product of gene 5 (gp5). In isolation, gp5 is a DNA polymerase of low processivity. However, gp5 becomes highly processive upon formation of a complex with Escherichia coli thioredoxin, the product of the trxA gene. Expression of a gp5 variant in which aspartate residues in the metal-binding site of the polymerase domain were replaced by alanine is highly toxic to E. coli cells. This toxicity depends on the presence of a functional E. coli trxA allele and T7 RNA polymerase-driven expression but is independent of the exonuclease activity of gp5. In vitro, the purified gp5 variant is devoid of any detectable polymerase activity and inhibited DNA synthesis by the replisomes of E. coli and T7 in the presence of thioredoxin by forming a stable complex with DNA that prevents replication. On the other hand, the highly homologous Klenow fragment of DNA polymerase I containing an engineered gp5 thioredoxin-binding domain did not exhibit toxicity. We conclude that gp5 alleles encoding inactive polymerases, in combination with thioredoxin, could be useful as a shutoff mechanism in the design of a bacterial cell-growth system.

Biochemical characterization of human DNA polymerase i provides clues to its biological function

2001 ◽  
Vol 29 (2) ◽  
pp. 183-187 ◽  
Author(s):  
A. Tissier ◽  
E. G. Frank ◽  
J. P. McDonald ◽  
A. Vaisman ◽  
A. R. Fernàndez deHenestrosa Henestrosa ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Biochemical Characterization ◽  
Short Review ◽  
Biochemical Properties ◽  
Dna Polymerase I ◽  
Polymerase I

The human RAD30B gene has recently been shown to encode a novel DNA polymerase, DNA polymerase i (poli). The role of poli within the cell is presently unknown, and the only clues to its cellular function come from its biochemical characterization in vitro. The aim of this short review is, therefore, to summarize the known enzymic activities of poli and to speculate as to how these biochemical properties might relate to its in vivo function.

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