l(2)34De, l(2)br16, MtPolB, pol γ-β, DNApol-γ
Gene model reviewed during 5.41
Gene model reviewed during 5.52
Multiphase exon postulated: this gene shares a region of coding sequence with an overlapping gene, but different reading frames are utilized in the overlapping coding region.
There is only one protein coding transcript and one polypeptide associated with this gene
Mitochondrial DNA polymerase was purified to near
homogeneity from early embryos. It is a heterodimer consisting of two
subunits of 125kD and 35kD. The large subunit contains the DNA-polymerase
activity.The DNA polymerase utilizes a large variety of template-primers
Component of the DNA polymerase gamma complex consisting of two subunits: the catalytic subunit DNApol-gamma/DNApolG1 and the accessory subunit DNApol-gamma35/DNApolG2.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\PolG2 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\PolG2 in GBrowse 2
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
Source for identity of: PolG2 DNApol-γ35
Source for merge of: MtPolB l(2)34De
Dicistronic annotation CG33084 split out into separate annotations for each open reading frame, CG33649 and CG33650 in release 4.2 of the genome annotation. CG33650 corresponds to DNApol-γ35.
Multiple amino acid sequence alignments show the DNA polymerases from numerous species forms a family strongly conserved from yeast to man.
Subunit structure and enzymatic activity of DNA polymerase γ are studied using a combination of physical and immunological approaches. The role of the 2 subunits in template primer DNA binding is explored.
The rate and processivity of DNA synthesis by DNA polymerase γ has been analysed under a variety of different conditions.
Biochemical description of the 3'->5' exonuclease associated with mitochondrial DNA polymerase.
The 3' to 5' exonuclease encoded provides a proof reading function to enhance the fidelity of DNA synthesis during mitochondrial DNA replication.
A structural and mechanistic analysis of DNApol-γ125 and DNApol-γ35 demonstrates them to be both effective and accurate in the synthesis of DNA.
Comparison of the rate and specificity of DNA synthesis by DNApol-γ125 and DNApol-γ35 on several template primers, and an examination of the products of DNA synthesis has been carried out.
DNApol-γ125 and DNApol-γ35 have been isolated and purified and their subunit structure and catalytic properties examined.