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Polymerase (RNA) III (DNA directed) Polypeptide H(POLR3H) is a member of the eukaryotic RPB7/RPC8 RNA polymerase subunit family. POLR3H is DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA utilizing the 4 ribonucleoside triphosphates as substrates. POLR3H has a central role in sensing and curbing infection by intracellular bacteria and DNA viruses. POLR3H functions as nuclear and cytosolic DNA sensor which is involved in innate immune response.

POLR2H is an essential and highly conserved subunit of RNA polymerase II which is shared by the other 2 eukaryotic DNA-directed RNA polymerases, I and III. The three eukaryotic RNA polymerases are complex multisubunit enzymes which play a vital role in the transcription of nuclear genes. POLR2H encodes an essential and highly conserved subunit of RNA polymerase II which is shared by the other two eukaryotic DNA-directed RNA polymerases, I and III.

Polymerase (RNA) I (DNA directed) Polypeptide C (POLR1C) is a subunit of both RNA polymerase I and RNA polymerase III complexes whose defects are related with Collins syndrome. POLR1C is a protein-coding gene and is part of the Pol core element

Polymerase (RNA) II (DNA directed) Polypeptide J (POLR2J) is a subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The POLR2J protein occurs as a heterodimer with another polymerase subunit; together they develop a core subassembly unit of the polymerase. POLR2J is ubiquitously expressed, having a high expression in the heart and skeletal muscle.

Polymerase (RNA) II (DNA directed) Polypeptide K, also knownas POLR2K is am ember of the archaeal RpoP/eukaryotic RPC10 RNA polymerase subunit family. POLR2K is one of the smallest subunits of RNA polymerase II, the polymerase is responsible for synthesizing messenger RNA in eukaryotes. In addition, the other two DNA-directed RNA polymerases share this subunit.

Polymerase III Polypeptide K, known as PORL3K, is a small vital subunit of RNA polymerase III. The carboxy-terminal domain of PORL3K owns a sequence which is very similar to the carboxy-terminal domain of an RNA polymerase II elongation factor. PORL3K takes part in sensing and limiting infection by intracellular bacteria and DNA viruses. PORL3K is also plays a role as nuclear and cytosolic DNA sensor which takes part in the innate immune response.

Polymerase (RNA) II (DNA directed) Polypeptide C (POLR2C) is the 3rd largest subunit of RNA polymerase II. The product of POLR2C consists of a cysteine rich area and exists as a heterodimer with an additional polymerase subunit, POLR2J. Those 2 subunits shape a core subassembly unit of the polymerase.

Polymerase III Polypeptide F (POLR3F) is a member of the eukaryotic RPC34/RPC39 RNA polymerase subunit family. POLR3F is DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA using the 4 ribonucleoside triphosphates as substrates. POLR3F is one of many subunits forming eukaryotic RNA polymerase III (RNA Pol III), which transcribes 5S ribosomal RNA and tRNA genes. POLR3F binds both TFIIIB90 and TBP, 2 subunits of RNA polymerase III transcription initiation factor IIIB (TFIIIB).

POLR2J2 belongs to the RNA polymerase II subunit 11 gene family, that includes 3 genes in a cluster on chromosome 7q22.1 and a pseudogene on chromosome 7p13. DNA directed RNA polymerase II polypeptide J family encodes a subunit of RNA polymerase II, the polymerase which is responsible for synthesizing messenger RNA in eukaryotes. This locus produces multiple, otherwise spliced transcripts which express isoforms with distinct C-termini compared to DNA directed RNA polymerase II polypeptide J. Most or all variants are spliced to include additional non-coding exons at the 3' end that makes them candidates for nonsense-mediated decay (NMD). Therefore, it is unknown if this locus expresses a protein or proteins in vivo.

Polymerase II Polypeptide I (POLR2I) is a member of the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family. POLR2I is a subunit of RNA polymerase II, which is a polymerase responsible for synthesizing messenger RNA in eukaryotes. DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the 4 ribonucleoside triphosphates as substrates. In addition POLR2I synthesizes mRNA precursors and numerous functional non-coding RNAs.

DNA-directed RNA polymerase II subunit RPB11-b2 (POLR2J3) is a member of the eukaryotic RPB11 RNA polymerase subunit family. POLR2J (DNA-directed RNA polymerase II subunit J) exists in 3 variants POLR2J1 (RPB11-a), POLR2J2 (RPB11-b1), and POLR2J3 (RPB11-b2). POLR2J3 is a DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

DNA-directed RNA polymerases I, II, and III subunit RPABC1 (POLR2E) is a member of the archaeal RpoH/eukaryotic RPB5 RNA polymerase subunit family. POLR2E being a DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the 4 ribonucleoside triphosphates as substrates. POLR2E is the 5th largest subunit of RNA polymerase II (the polymerase which is responsible for synthesizing messenger RNA in eukaryotes). The POLR2E subunit is shared by the other 2 DNA-directed RNA polymerases and is present in two-fold molar excess over the other polymerase subunits. An interaction between the POLR2E subunit and a hepatitis virus transactivating protein has been established, suggesting that an interaction between transcriptional activators and the polymerase can occur through the POLR2E subunit.

Polymerase II Polypeptide F (POLR2F) is the 6th largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes, which is also shared by the other two DNA-directed RNA polymerases. In yeast, POLR2F, in combination with at least 2 other subunits, forms a structure which stabilizes the transcribing polymerase on the DNA template. DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA via the 4 ribonucleoside triphosphates as substrates. Pol II is the principal element of the basal RNA polymerase II transcription apparatus. Pols are comprised of mobile elements which move close to each other. In Pol II, POLR2F/RPB6 is part of the clamp element and along with parts of RPB1 and RPB2 constructs a compartment to which the RPB4-RPB7 subcomplex attaches.

Polymerase (DNA Directed), Epsilon 3, also know as POLE3, is a histone-fold protein which interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers merge into larger enzymatic complexes for DNA transcription, replication, and packaging.

Polymerase II Polypeptide D (POLR2D) is a member of the eukaryotic RPB4 RNA polymerase subunit family. POLR2D is the fourth largest subunit of RNA polymerase II. Pol II is the main element of the basal RNA polymerase II transcription machinery. polymerase is responsible forsynthesizing messenger RNA in eukaryotes. In yeast, POLR2D subunit is connected with the polymeraseunder suboptimal growth conditions and might have a stress protective role. POLR2D catalyzes the transcription of DNA into RNA by the 4 ribonucleoside triphosphates as substrates.

T7 RNA polymerase active enzyme synthesizes RNA at an increasing degree of that of E. coli RNA polymerase and it terminates transcription often. T7 RNA polymerase is very selective for initiation at its own promoter sequences and is resistant to antibiotics that inhibit E. coli RNA polymerase. In-vitro transcription of mRNA is achieved via bacteriophage T7 RNA polymerase using its ability to produce full-length RNA transcripts with high reliability, thoughT7 RNAP can manufacture as well immunostimulatory by products for example dsRNA which affect protein expression.

DNA polymerase POLL is involved in base excision repair (BER). POLL is a low-fidelity polymerase that takes part in both spontaneous and DNA damage-induced mutagenesis. Furthermore, POLL takes part in the mutagenic bypass of T-T dimers. Pol lambda possesses terminal transferase and 5’-deoxyribose-5-phosphate lyase activity which is synchronized by PCNA and replication protein A.

Pfu DNA polymeraseenzyme is found in the hyperthermophilic archaeonPyrococcus furiosus, where it functions in vivoto replicate the organism's DNA. In vitro, Pfu is used to swiftly amplify DNAin the Polymerase Chain Reaction, where the enzyme serves the central function of copying a new strand of DNA during each extension step. Pfu DNA polymerase has superior thermostability and 'proofreading' properties compared to other thermostable polymerases. Unlike Taq DNA polymerase, Pfu DNA polymerase possesses 3' to 5' exonuclease proof reading activity, meaning that it works its way along the DNA from the 5' endto the 3' endand corrects nucleotidemisin corporation errors. Pfu DNA polymerase-generated PCRfragments will have fewer errors than Taq-generated PCR inserts. As a result, Pfu is more commonly used for molecular cloning of PCR fragments than the historically popular Taq. Pfu DNA polymerase is superior for techniques that require high-fidelity DNA synthesis, but can also be used in conjunction with Taq polymerase to obtain the fidelity of Pfu with the speed of Taq polymerase activity.

DNA polymerase beta (POLB) is a member of the DNA polymerase type-X family. In eukaryotic cells, POLB performs base excision repair necessary for DNA maintenance, replication, recombination, and drug resistance. POLB has 2 separate domains; the larger is the polymerase domain itself, whereas a small basic N-terminal domain contains an AP lyase activity which excises the abasic sugar-phosphate residue at the strand break. POLB fills single nucleotide gaps in DNA produced by the base excision repair pathway of mammalian cells. POLB overexpression, as seen in some human tumors, could convene an increase in spontaneous mutagenesis.

TAF10 is a small subunit of TFIID which is related to a subdivision of TFIID complexes. Studies with human and mammalian cells verified that this subunit is mandatory for transcriptional activation by the estrogen receptor, for progression through the cell cycle, and is essential for several cellular differentiation programs.

CRCP is a ubiquitous coupling protein for the calcitonin gene-related peptide and adrenomedullin receptors. CRCP controls ligand sensitivity in several tissues and has DNA-directed RNA polymerase activity, catalytic activity and calcitonin receptor activity.

REV1 Polymerase (REV1) contains a BRCT domain, which is imperative in protein-protein interactions. REV1 is a deoxycytidyl transferase involved in DNA repair. REV1 assists in the 1st step in the bypass of abasic lesions by the incorporation of a nucleotide opposite the lesion. REV1 is essential for normal generation of mutations by physical and chemical agents. REV1 transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. A role for the human Rev1-like protein has been suggested as a scaffold which recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA.

SSU72 is an extremely conserved homologue of yeast Ssu72, a CTD phosphatase and a component of the polyadenylation/termination machinery. SSU72 interacts with TFIIB, Rb and DNAM-1 and operates to catalyze the dephosphorylation of target proteins, and taking part in RNA processing and termination via dephosphorylation of Pol II. SSU72 is found in multiple alternatively spliced isoforms.