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DNA primase large subunit is an enzyme that in humans is encoded by the PRIM2 gene. [ 5 ] [ 6 ] The replication of DNA in eukaryotic cells is carried out by a complex chromosomal replication apparatus, in which DNA polymerase alpha and primase are two key enzymatic components.
Shared primase-binding peptide in archaeal PolD and eukaryotic Polα [1] DNA polymerase alpha also known as Pol α is an enzyme complex found in eukaryotes that is involved in initiation of DNA replication. The DNA polymerase alpha complex consists of 4 subunits: POLA1, POLA2, PRIM1, and PRIM2. [2]
DNA primase is an enzyme involved in the replication of DNA and is a type of RNA polymerase. Primase catalyzes the synthesis of a short RNA (or DNA in some living organisms [ 1 ] ) segment called a primer complementary to a ssDNA (single-stranded DNA) template.
Not only is the general topology conserved, the two also share a bifunctional primase-and-PCNA-binding PIP-box sequence on the C-terminus, similar to both eukaryotic Polα and Polε. [37] In 1998, the family D of DNA polymerase was discovered in Pyrococcus furiosus and Methanococcus jannaschii. [38]
18968 Ensembl ENSG00000101868 ENSMUSG00000006678 UniProt P09884 P33609 RefSeq (mRNA) NM_016937 NM_001330360 NM_001378303 NM_008892 RefSeq (protein) NP_001317289 NP_058633 NP_001365232 NP_032918 Location (UCSC) Chr X: 24.69 – 25 Mb Chr X: 92.35 – 92.68 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse DNA polymerase alpha catalytic subunit is an enzyme that in humans is encoded by ...
[5] [6] [7] PrimPol is a eukaryotic protein with both DNA polymerase and DNA Primase activities involved in translesion DNA synthesis. It is the first eukaryotic protein to be identified with priming activity using deoxyribonucleotides. [6] [7] It is also the first protein identified in the mitochondria to have translesion DNA synthesis activities.
Transcription preinitiation complex, represented by the central cluster of proteins, causes RNA polymerase to bind to target DNA site. The PIC is able to bind both the promoter sequence near the gene to be transcribed and an enhancer sequence in a different part of the genome, allowing enhancer sequences to regulate a gene distant from it.
The E. Coli DnaG primase is a 581 residue monomeric protein with three functional domains, according to proteolysis studies. There is an N-terminal Zinc-binding domain (residues 1–110) where a zinc ion is tetrahedrally coordinated between one histidine and three cysteine residues, which plays a role in recognizing sequence specific DNA binding sites.