Catalytic subunit of DNA polymerase gamma solely responsible for replication of mitochondrial DNA (mtDNA). Replicates both heavy and light strands of the circular mtDNA genome using a single-stranded DNA template, RNA primers and the four deoxyribonucleoside triphosphates as substrates . Has 5' -> 3' polymerase activity. Functionally interacts with TWNK and SSBP1 at the replication fork to form a highly processive replisome, where TWNK unwinds the double-stranded DNA template prior to replication and SSBP1 covers the parental heavy strand to enable continuous replication of the entire mitochondrial genome. A single nucleotide incorporation cycle includes binding of the incoming nucleotide at the insertion site, a phosphodiester bond formation reaction that extends the 3'-end of the primer DNA, and translocation of the primer terminus to the post-insertion site. After completing replication of a mtDNA strand, mediates 3' -> 5' exonucleolytic degradation at the nick to enable proper ligation . Highly accurate due to high nucleotide selectivity and 3' -> 5' exonucleolytic proofreading. Proficiently corrects base substitutions, single-base additions and deletions in non-repetitive sequences and short repeats, but displays lower proofreading activity when replicating longer homopolymeric stretches. Exerts exonuclease activity toward single-stranded DNA and double-stranded DNA containing 3'-terminal mispairs. When a misincorporation occurs, transitions from replication to a pro-nucleolytic editing mode and removes the missincorporated nucleoside in the exonuclease active site. Proceeds via an SN2 nucleolytic mechanism in which Asp-198 catalyzes phosphodiester bond hydrolysis and Glu-200 stabilizes the leaving group. As a result the primer strand becomes one nucleotide shorter and is positioned in the post-insertion site, ready to resume DNA synthesis . Exerts 5'-deoxyribose phosphate (dRP) lyase activity and mediates repair-associated mtDNA synthesis (gap filling) in base-excision repair pathway. Catalyzes the release of the 5'-terminal 2-deoxyribose-5-phosphate sugar moiety from incised apurinic/apyrimidinic (AP) sites to produce a substrate for DNA ligase. The dRP lyase reaction does not require divalent metal ions and likely proceeds via a Schiff base intermediate in a beta-elimination reaction mechanism . .

DNA polymerase subunit gamma-1 (EC 2.7.7.7) (3'-5' exodeoxyribonuclease) (EC 3.1.11.-) (5'-deoxyribose-phosphate lyase) (EC 4.2.99.-) (Mitochondrial DNA polymerase catalytic subunit) (PolG-alpha) POLG MDP1 POLG1 POLGA

Rat;Pig;Human

WB,IHC

WB 1:100-1:500
IHC 1:50-1:200

139.562kD;

POLG MDP1 POLG1 POLGA

p54098

https://www.uniprot.org/uniprotkb/p54098

RKRF72349-Recombinant Polymerase DNA Directed Gamma 1 (POLg1) Trp1041~Pro1239

Rabbit

Polyclonal

Rabbit IgG

Enzyme Kinase;

Antigen-specific affinity chromatography followed by Protein A affinity chromatography

Liquid

500μg/mL

0.01M PBS, pH7.4, containing 0.05% Proclin-300, 50% glycerol.

Store at +4℃ after thawing. For long-term storage, please store it at -20℃. Avoid repeated freeze / thaw cycles.