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).
Nyren P., 1987: Enzymatic method for continuous monitoring of dna polymerase activity. Analytical Biochemistry: 235-238 A simple and rapid method for the assay of Dna polymerase activity has been developed. The PPi formation in the Dna polymerase reaction is continuously monitored by a coupled enzymatic method (P. Nyren and A. Lundin, 1985, Anal. Biochem. 151 [...]
Ehrenfeld E., 1988: Enzymatic activity of poliovirus rna polymerase synthesized in escherichia coli from viral complementary dna. Virology: 301-308 Plasmids have been constructed that contain Dna sequences that direct the expression of the poliovirus Rna-dependent Rna polymerase, in the form of recombinant fusion proteins. Inclusion of an additional gene for the poliovirus protease results in [...]
Modak M.J., 1980: Enzymatic activities associated with avian and murine retroviral dna polymerases catalysis of and active site involvement in pyro phosphate exchange and pyro phosphorolysis reactions. Journal Of Biological Chemistry: 2000-2004 Reverse transcriptase isolated from avian myeloblastosis virus (Amv) and Rauscher murine leukemia virus (Rlv) were examined for their ability to catalyze polymerization. RNase [...]
Studier F.W., 1988: Entry of bacteriophage t7 dna into the cell and escape from host restriction. Journal Of Bacteriology: 2095-2105 T7 Dna did not become susceptible to degradation by the host restriction enzymes EcoB, EcoK, or EcoP1 until 6 to 7 min after infection (at 30.degree. C). During this period, T7 gene 0.3 protein is [...]
Kamikubo T., 1983: Enhancement of template activity of chromatin in pea pisum sativum cultivar alaska by gibberellic acid. Plant Science Letters: 155-164 Chromatin was prepared from 8-day-old pea seedlings (P. sativum cv. Alaska) which had been treated with Ga3 for 48 h or 0 h, and its template activity was measured using a purified cauliflower [...]
Duffy J.J., 1979: Enhanced transcription by rna polymerase ii and rna polymerase iii after inhibition of protein synthesis. Journal Of Biological Chemistry: 4154-4156 Administration of cycloheximide (100 mg/kg) ip to rats produces a time-dependent rise in nuclear Rna polymerase Ii activity which is maximum at 30 min. This same concentration of cycloheximide also reduces Rna [...]
Berezney R., 1987: Enhanced processivity of nuclear matrix bound dna polymerase alpha from regenerating rat liver. Biochemistry: 5710-5718 Translocation of Dna during in vitro Dna synthesis on nuclear matrix bound replicational assemblies from regenerating rat liver was determined by measuring the processivity (average numer of nucleotides added following one productive binding event of the polymerase [...]
Kouidou, S.; Triantos, A.; Kavoukopoulos, E.; Trakatellis, A., 1981: Endoplasmic reticulum nuclease ec 3.1.3 purification and specificity. European Journal of Biochemistry 120(1): 9-14 An endonuclease, which was originally identified for its Rna polymerase inhibitory activity, was isolated from rat liver endoplasmic reticulum. The enzyme yields on gel chromatography 4 active fractions of different Mw (Mw [...]
Nava C., 1980: Emt 6 solid tumor growth dna synthesis and dna polymerase activity. Cancer Biochemistry Biophysics: 55-62 Serial Dna-polymerase-.alpha. and -.beta. enzyme level measurements were made during the growth of the Emt6 solid tumor. The determinations were correlated with Dna-synthesis in the tumor as measured by 3h-TdR labeling. The Dna-.alpha. polymerase levels were initially [...]
Burgess R.R., 1980: Elution of proteins from sodium dodecyl sulfate poly acrylamide gels removal of sodium dodecyl sulfate and renaturation of enzymatic activity results with sigma subunit of escherichia coli rna polymerase wheat germ dna topo isomerase and other enzymes. Analytical Biochemistry: 76-86 An improved method is described for the renaturation of microgram amounts of [...]