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Literature summary for 5.6.2.3 extracted from

  • Ciesielski, G.L.; Nadalutti, C.A.; Oliveira, M.T.; Jacobs, H.T.; Griffith, J.D.; Kaguni, L.S.
    Structural rearrangements in the mitochondrial genome of Drosophila melanogaster induced by elevated levels of the replicative DNA helicase (2018), Nucleic Acids Res., 46, 3034-3046 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.3

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of the helicase in Drosophila melanogaster Schneider S2 cells, the elevated enzyme levels induce structural rearrangements in the mitochondrial genome of Drosophila melanogaster Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
additional information overexpression of the enzyme in Schneider S2 cells, elevated levels of mtDNA helicase alleviate pausing of the replication fork and increase the abundance of replication intermediates. The substantial increase in the signal of RIs in the absence of mtDNA copy number changes suggests that overexpression of mtDNA helicase promotes increased initiation without complete replication of mtDNA molecules. Circular molecules bear deletions in mtDNA from helicase overexpressing cells, elevated levels of mtDNA helicase promote rearrangement of the A+T region, mechanism, overview Drosophila melanogaster

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Drosophila melanogaster 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Drosophila melanogaster

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Drosophila melanogaster
-
 ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster Q9VL76
-
-

Source Tissue

Source Tissue Comment Organism Textmining
S2 cell
-
 Drosophila melanogaster
-
SCHNEIDER-2 cell
-
 Drosophila melanogaster
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Drosophila melanogaster ADP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
mtDNA helicase
-
 Drosophila melanogaster
replicative DNA helicase
-
 Drosophila melanogaster

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Drosophila melanogaster

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Drosophila melanogaster

General Information

General Information Comment Organism
malfunction mtDNA helicase mutations are associated with structural rearrangements of the mitochondrial genome, elevation of mtDNA helicase levels increases the quantity of replication intermediates and alleviates pausing at the replication slow zones. A concomitant alteration in mtDNA copy number is not observed, but deletions specific to the segment of repeated elements in the immediate vicinity of the origin of replication, and an accumulation of species characteristic of replication fork stalling. Elevated levels of RNA that are retained in the replication intermediates are also found. Effects of elevated levels of the mtDNA helicase on the integrity and replication of the mitochondrial genome, overview Drosophila melanogaster
metabolism pathological conditions impairing functions of mitochondria often lead to compensatory upregulation of the mitochondrial DNA (mtDNA) replisome machinery, and the replicative DNA helicase appears to be a key factor in regulating mtDNA copy number. Upregulation of mtDNA helicase promotes the process of mtDNA replication but also results in genome destabilization Drosophila melanogaster
physiological function the enzyme is involved in the replication of the mitochondrial genome. Replication of mtDNA requires two key mitochondrial enzymes: DNA polymerase gamma (Pol gamma) and mtDNA helicase. Upregulation of mtDNA helicase promotes the process of mtDNA replication but also results in genome destabilization Drosophila melanogaster