A polymerase is basically an enzyme associated with polymers of nucleic acids such as the deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). The main function of a polymerase is to polymerize new DNA or RNA against a currently existing DNA or RNA template, as seen in the processes of nucleic acid replication and transcription. Polymerases also take nucleotides from solvent and bring about the synthesis of polynucleotide sequences against a nucleotide template strand, through using base-pairing interactions. This secondary function is observable when polymerases are associated with a cluster of other enzymes and proteins.
Common polymerases include the terminal deoxynucleotidyl transferase (also known as TDT), which often gives a bit of diversity to chains that are heavy with antibodies, and the reverse transcriptase, which is an enzyme found in RNA retroviruses (such as HIV) and is used to create a complementary strand to the existing strand of viral RNA before effectively integrating into the host cell’s DNA.
There are other kinds of polymerases that are specific to the nucleic acids, such as the DNA polymerase, which aids in catalyzing the polymerization of DNA bases (known as deoxyribonucleotides) into a DNA strand. DNA polymerases are subdivided into seven different families: Family A, Family B, Family C, Family D, Family X, Family Y, and Family RT.
RNA polymerases are specific to RNA strands, and these polymerases are also known as DNA-dependent RNA polymerase. These enzymes are essential in producing RNA strands, as well as constructing RNA chains through the use of DNA genes as the basic templates. This process is known as transcription. RNA polymerases are very important to all kinds of all living organisms, and even viruses as well.
This category contains scientific information on polymerase, an enzyme associated with polymers of nucleic acids such as the deoxyribonucleic acid (DNA) and ribonucleic acid (RNA).
Buchowicz J., 1983: Preferential stimulation of rna polymerase iib by a chromosomal protein from wheat triticum aestivum germ. Phytochemistry (oxford): 1707-1712 An Rna polymerase Ii stimulatory protein was purified from wheat germ chromatin and tested for the ability to stimulate wheat germ Rna polymerases I, Iia, Iib and Ii The form Iib of the class [...]
Collins J.M., 1986: Preferential binding of dna primase to the nuclear matrix in hela cells. Journal Of Biological Chemistry6: 7119-7123 Studies of the spatial organization of Dna replication have provided increasing evidence of the importance of the nuclear matrix. We have previously reported a relationshp between rates of Dna synthesis and the differential binding of [...]
Shadley J.D., 1986: Potentiation of sister chromatid exchange by 3 aminobenzamide is not modulated by topoisomerases or proteases. Environmental Mutagenesis: 487-494 Poly(Adp-ribose) is synthesized in response to Dna strand breaks and covalently modifies numerous intracellular proteins. We have proposed that this modification regulates, i.e., inhibits, the activity of these enzymes, e.g., topoisomerases and proteases, which [...]
Parthier B., 1985: Polypeptides of dna dependent rna polymerase of spinach chloroplasts characterization by antibody linked polymerase assay and determination of sites of synthesis. Embo (european Molecular Biology Organization) Journal: 1661-1666 Using solid-phase Sandwich immunoassays Dna-dependent Rna polymerase of spinach chloroplasts was studied with regard to polypeptide composition of the multimeric enzyme, immunological cross-reaction with [...]
Smulson M., 1983: Polyoma virus mini chromosomes poly adp ribosylation of associated chromatin proteins. Journal Of Virology: 600-606 The host nuclear enzyme poly(Adp-ribose) polymerase was shown to be associated with the replicative intermediate and mature forms of polyoma virus minichromosomes. Minichromosome-associated histones H2a and H2b and several nonhistone proteins were poly Adp-ribosylated by endogenous poly(Adp-ribose) [...]
Levine M.J., 1985: Polymorphic radiation sensitivity of human natural killer activity possible role of dna strand breakage. Human Immunology: 49-58 Natural killer (Nk) activity of human mononuclear cells in sensitive to inhibition by radiation, under the control of polymorphic X-linked genes. To define the mechanism of this inhibition, the ability of treatments known to damage [...]
Papamichail M., 1987: Polyadenylic acid metabolizing enzyme levels during induction of differentiation in a human leukemia t cell line with phorbol ester. Jnci (journal Of The National Cancer Institute): 407-412 Induction of differentiation of Molt3 cells with 12-O-tetradecanoylphorbol-13-acetate (Tpa) was found to affect the activity levels of the polyadenylic acid metabolizing enzymes. Tpa administration at [...]
Bacchi C.J., 1981: Poly amines stimulate dna directed dna synthesis catalyzed by mammalian type c retroviral dna polymerases. Journal Of Biological Chemistry: 3460-3464 In the presence of optimal concentrations of Mg2+, rates of activated (gapped) Dna-directed Dna synthesis by purified mammalian type C retroviral Dna polymerases are stimulated greater than 10-fold by the polyamines spermine [...]
Holland J.M., 1982: Poly adp ribosylation in n n di ethyl nitrosamine treated mice. International Journal Of Biochemistry: 231-234 Liver nuclei isolated from male mice treated with the carcinogen, N,N-diethylnitrosamine, were examined for the homopolymer poly(adenosine diphosphate ribose) and for the activity of the conjugate polymerase. At all levels of the carcinogen tested, a concomitant [...]