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).
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 [...]
Delain E., 1983: Poly adp ribose polymerase auto modification and interaction with dna electron microscopic visualization. Embo (european Molecular Biology Organization) Journal: 543-548 The interaction between purified calf thymus poly(Adp-ribose) polymerase and its activating co-purified Dna (sDNA) was investigated by Em. The enzyme-Dna complex possesses a nucleosome-like structure. The enzyme-bound Dna (sDNA) was found to [...]
Sheinin R., 1981: Poly adp ribose polymerase activity in mouse cells which exhibit temperature sensitive dna synthesis. Biochimica Et Biophysica Acta: 271-275 The poly(Adp-ribose) polymerase activity of wild-type mouse L cells and of Balb/C-3t3 mouse fibroblasts remained relatively unchanged (at.apprx. 400 nmol substrate utilized/mg Dna per h) in actively-growing cells incubated at 34.degree. C or [...]
Mandel P., 1981: Poly adp ribose polymerase activity in neuronal and glial nuclei from bovine cerebrum. Neurochemical Research: 1253-1264 Two different preparations isolated from beef cerebrum were used to compare the poly Adp-ribose (polyADPR) polymerase activities in neuronal and glial nuclei: Nuclear suspensions (with or without DNase 1 treatment), and 1 M NaCl nuclear extracts [...]
Althaus F.R., 1987: Poly adp ribose may signal changing metabolic conditions of the chromatin of mammalian cells. Proceedings Of The National Academy Of Sciences Of The United States Of America: 1286-1289 In mammalian cells, Nad+ serves a dual role as a respiratory coenzyme and as a substrate for the posttranslational poly(Adp-ribose) modification of chromatin proteins, [...]
“Gill D.M., 1988: Poly adp ribose degradation by glycohydrolase starts with an endonucleolytic incision. Journal Of Biological Chemistry3: 11037-11040 We have recently shown that poly(Adp-ribose) polymerase forms poly(Adp-ribose) by adding Adp-ribose residues to the polymerase-proximal end of an enzyme-bound nascent chain. In this light we have reexamined the mode of hydrolysis of enzyme-bound poly(Adp-ribose) by [...]
Poirier G.G., 1986: Poly adp ribose accessibility to poly adp ribose glycohydrolase activity on poly adp ribosylated nucleosomal proteins. Canadian Journal Of Biochemistry & Cell Biology: 146-153 Hydrolysis of protein-bound 32p-labelled poly(Adp-ribose) by poly(Adp-ribose) glycohydrolase shows that there is differential accessibility of poly(Adp-ribosyl)ated proteins in chromatin to poly(Adp-ribose)glycohydrolase. The rapid hydrolysis of hyper(Adp-ribosyl)ated forms of [...]
Dennis, J.; Kisilevsky, R., 1980: Poly adenylic acid polymerase ec 188.8.131.52 activity in ethionine intoxicated rats the relative effectiveness of disaggregated and intact poly ribosomes as primers for poly adenylic acid polymerase. Canadian Journal of Biochemistry 58(3): 236-242 Ethionine intoxication causes a change in the metabolism of poly(A) sequences on the 3′ Oh terminus of [...]
Lucchini, R.; Vezzoni, P.; Giardini, R.; Vezzoni, M. A.; Raineri, M.; Clerici, L., 1984: Poly adenylic acid polymerase ec 184.108.40.206 distribution in normal and malignant lymphoid cells. Tumori 70(2): 141-146 The incorporation of Atp on poly(A) primers catalyzed by poly(A) polymerase was investigated in normal and neoplastic lymphoid cells from animal and human sources. High [...]