Bridging PNAs can bind preferentially to a deleted mitochondrial DNA template but replication by mitochondrial DNA polymerase γ in vitro is not impaired

2003 ◽  
Vol 1629 (1-3) ◽  
pp. 73-83 ◽  
Author(s):  
Alistair McGregor ◽  
Paul M. Smith ◽  
Günther F. Ross ◽  
Robert W. Taylor ◽  
Douglass M. Turnbull ◽  
...  
Keyword(s):  
Mitochondrial Dna ◽  
Dna Polymerase ◽  
Dna Template ◽  
Mitochondrial Dna Polymerase ◽  
Dna Polymerase Γ

scholarly journals Properties of mitochondrial DNA polymerase in mitochondrial DNA synthesis in yeast.

1995 ◽  
Vol 42 (3) ◽  
pp. 317-324 ◽  
Author(s):  
T K Biswas ◽  
P Sengupta ◽  
R Green ◽  
P Hakim ◽  
B Biswas ◽  
...  
Keyword(s):  
Mitochondrial Dna ◽  
Dna Synthesis ◽  
Dna Polymerase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Mt Dna ◽  
Double Stranded Dna ◽  
Dna Template ◽  
Mitochondrial Dna Polymerase

Mitochondrial DNA polymerase from Saccharomyces cerevisiae, purified 3500 fold, was separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis into three polypeptides. The major 150 kDa polypeptide was probably the catalytic subunit of the mitochondrial (mt) DNA polymerase and the other two polypeptides could be either proteolytic cleavage products of the polymerase, other subunits of the enzyme or protein contaminants. The mtDNA polymerase preferred an A+T-rich DNA template and did not require any RNA primer for DNA synthesis, at least under in vitro reaction conditions. It showed higher processivity on a double-stranded linear DNA template than on a single-stranded circular DNA template, and was capable of synthesizing at least about 1200 nucleotide primer-extended products without any major pause on a double-stranded DNA template.

scholarly journals Mitochondrial DNA polymerase-γ and human disease

2006 ◽  
Vol 15 (suppl_2) ◽  
pp. R244-R252 ◽  
Author(s):  
Gavin Hudson ◽  
Patrick F. Chinnery
Keyword(s):  
Mitochondrial Dna ◽  
Dna Polymerase ◽  
Human Disease ◽  
Mitochondrial Dna Polymerase ◽  
Dna Polymerase Γ

Genomic Structure of Murine Mitochondrial DNA Polymerase-γ

2000 ◽  
Vol 19 (10) ◽  
pp. 601-605 ◽  
Author(s):  
Justin L. Mott ◽  
Grace Denniger ◽  
Steve J. Zullo ◽  
H. Peter Zassenhaus
Keyword(s):  
Mitochondrial Dna ◽  
Dna Polymerase ◽  
Genomic Structure ◽  
Mitochondrial Dna Polymerase ◽  
Dna Polymerase Γ

scholarly journals A novel interaction between DNA ligase III and DNA polymerase γ plays an essential role in mitochondrial DNA stability

2007 ◽  
Vol 402 (1) ◽  
pp. 175-186 ◽  
Author(s):  
Ananya De ◽  
Colin Campbell
Keyword(s):  
Mitochondrial Dna ◽  
Dna Polymerase ◽  
Mitochondrial Protein ◽  
Dna Ligase ◽  
Zinc Finger Domain ◽  
Wild Type ◽  
Mitochondrial Dna Copy Number ◽  
Dna Polymerase Γ ◽  
Dna Ligase Iii

The data in the present study show that DNA polymerase γ and DNA ligase III interact in mitochondrial protein extracts from cultured HT1080 cells. An interaction was also observed between the two recombinant proteins in vitro. Expression of catalytically inert versions of DNA ligase III that bind DNA polymerase γ was associated with reduced mitochondrial DNA copy number and integrity. In contrast, overexpression of wild-type DNA ligase III had no effect on mitochondrial DNA copy number or integrity. Experiments revealed that wild-type DNA ligase III facilitates the interaction of DNA polymerase γ with a nicked DNA substrate in vitro, and that the zinc finger domain of DNA ligase III is required for this activity. Mitochondrial protein extracts prepared from cells overexpressing a DNA ligase III protein that lacked the zinc finger domain had reduced base excision repair activity compared with extracts from cells overexpressing the wild-type protein. These data support the interpretation that the interaction of DNA ligase III and DNA polymerase γ is required for proper maintenance of the mammalian mitochondrial genome.

scholarly journals Functional Human Mitochondrial DNA Polymerase γ Forms a Heterotrimer

2005 ◽  
Vol 281 (1) ◽  
pp. 374-382 ◽  
Author(s):  
Elena Yakubovskaya ◽  
Zhixin Chen ◽  
José A. Carrodeguas ◽  
Caroline Kisker ◽  
Daniel F. Bogenhagen
Keyword(s):  
Mitochondrial Dna ◽  
Dna Polymerase ◽  
Human Mitochondrial Dna ◽  
Mitochondrial Dna Polymerase ◽  
Dna Polymerase Γ

scholarly journals Acute and Delayed Toxicity Studies on the Antiherpesvirus Agents 5-Methoxymethyl-2′-Deoxycytidine and 5-Methoxymethyl-2′-Deoxyuridine

1997 ◽  
Vol 8 (5) ◽  
pp. 439-442
Author(s):  
R Shi ◽  
SV Gupta ◽  
M Kukhanova ◽  
SVP Kumar ◽  
AL Stuart ◽  
...  
Keyword(s):  
Mitochondrial Dna ◽  
Dna Polymerase ◽  
Doubling Time ◽  
Prolonged Exposure ◽  
Potent Inhibitor ◽  
Control Drug ◽  
Delayed Toxicity ◽  
Simplex Virus ◽  
Mitochondrial Dna Polymerase ◽  
Dna Polymerase Γ

5-Methoxymethyl-2′-deoxycytidine (MMdCyd) and the corresponding deoxyuridine analogue, 5-methoxymethyl-2′-deoxyuridine (MMdUrd) are selective antiherpesvirus agents. MMdCyd (ED50 1.5 μM) is a more potent inhibitor of herpes simplex virus replication than MMdUrd (ED50 30 μM) when maintained in the deoxycytidine form (deamination prevented). The 5′-triphos-phates, MMdCTP and MMdUTP, were synthesized, and incorporation into DNA by mitochondrial DNA polymerase γ was investigated. MMdCTP and MMdUTP were incorporated into DNA in place of dCTP and dTTP, respectively. The effect of MMdCyd and MMdUrd on cell growth (acute toxicity) and prolonged exposure (delayed cytotoxicity) in CEM cells was investigated. The two analogues did not exhibit acute or delayed toxicity (2 weeks exposure) up to 1000 μM. In contrast, at a concentration as low as 0.125 μM of 2′,3′-dideoxycytidine (ddC; control drug), the doubling time of the cells increased after 10 days. At higher concentrations, a very marked increase in doubling time was observed from 6 days onward with ddC treatment. The data suggest that in uninfected cells neither MMdUrd nor MMdCyd are anabolized to the triphosphate form in significant amounts. As a result, little or no MMdCTP or MMdUTP builds up in the mitochondria and thus delayed toxicity is not observed.

scholarly journals Synergistic Effects of thein cisT251I and P587L Mitochondrial DNA Polymerase γ Disease Mutations

2017 ◽  
Vol 292 (10) ◽  
pp. 4198-4209 ◽  
Author(s):  
Karen L. DeBalsi ◽  
Matthew J. Longley ◽  
Kirsten E. Hoff ◽  
William C. Copeland
Keyword(s):  
Mitochondrial Dna ◽  
Dna Polymerase ◽  
Synergistic Effects ◽  
Disease Mutations ◽  
Mitochondrial Dna Polymerase ◽  
Dna Polymerase Γ

scholarly journals Atomistic Molecular Dynamics Simulations of Mitochondrial DNA Polymerase γ: Novel Mechanisms of Function and Pathogenesis

Biochemistry ◽  
2017 ◽  
Vol 56 (9) ◽  
pp. 1227-1238 ◽  
Author(s):  
Liliya Euro ◽  
Outi Haapanen ◽  
Tomasz Róg ◽  
Ilpo Vattulainen ◽  
Anu Suomalainen ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Mitochondrial Dna ◽  
Molecular Dynamics Simulations ◽  
Dna Polymerase ◽  
Dynamics Simulations ◽  
Mitochondrial Dna Polymerase ◽  
Dna Polymerase Γ
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