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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.
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.
19076 Ensembl ENSG00000146143 ENSMUSG00000026134 UniProt P49643 P33610 RefSeq (mRNA) NM_000947 NM_001282487 NM_001282488 NM_008922 RefSeq (protein) NP_000938 NP_001269416 NP_001269417 NP_032948 Location (UCSC) Chr 6: 57.31 – 57.65 Mb Chr 1: 33.49 – 33.71 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse DNA primase large subunit is an enzyme that in humans is encoded by the PRIM2 ...
A diagram showing where RNA primers bind to begin replication. [1]A primer binding site is a region of a nucleotide sequence where an RNA or DNA single-stranded primer binds to start replication.
A pre-replication complex (pre-RC) is a protein complex that forms at the origin of replication during the initiation step of DNA replication. Formation of the pre-RC is required for DNA replication to occur. Complete and faithful replication of the genome ensures that each daughter cell will carry the same genetic information as the parent cell.
T7 DNA helicase (gp4) is a hexameric motor protein encoded by T7 phages that uses energy from dTTP hydrolysis to process unidirectionally along single stranded DNA, separating the two strands as it progresses. It is also a primase, making short stretches of RNA that initiates DNA synthesis. [2] It forms a complex with T7 DNA polymerase.
[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.
c The cPIP of DP2 resembles the primase-interacting motif located in the C terminus of Polα. Top panel: multiple-sequence alignment highlighting the conservation between the PolD cPIP motifs from Thermococcus species and the primase-interacting peptides of Polα. Sequence similarities are highlighted with light purple boxes, whereas conserved ...