4 edition of Inhibitors of DNA and Rna Polymerases (International Encyclopaedia of Pharmacology) found in the catalog.
Inhibitors of DNA and Rna Polymerases (International Encyclopaedia of Pharmacology)
Prem S. Sarin
by Pergamon Pr
Written in English
|The Physical Object|
|Number of Pages||266|
RNA polymerase (ribonucleic acid polymerase), both abbreviated RNAP or RNApol, official name DNA-directed RNA polymerase (ribonucleic acid polymerase), both abbreviated RNAP or RNApol, official name DNA-directed RNA polymerase. For DNA polymerases to properly carry out their function they must have the following components present for catalysis to occur. 1. A template of DNA. The preferable template is a double stranded DNA. Single stranded DNA may also work as a template but RNA strands or DNA-RNA hybrids may not be used. 2. Activated precursors.
Inhibition of Nucleic Acid Synthesis. In a bacterial cell, or any kind of cell for that matter, the nucleic acids DNA and RNA are incredibly important molecules. DNA synthesis by two mechanisms that are generally associated: 1/ direct interference with molecules required for DNA polymerization or/and initiation of replication; and 2/ checkpoint response(s). The direct sites of drug action (“pharmacological targets”: nucleotide precursor pools, chain elongation, DNA polymerases, the DNA template, and.
The RNA pol involved in the synthesis of messenger RNA or DNA transcription. The RNA polymerase is the enzyme known soluble larger as measured about Å in diameter and is visible in electron micrographs, which notes attached to the promoter DNA. RNA polymerase (ribonucleic acid polymerase), abbreviated RNAP or RNApol, officially DNA-directed RNA polymerase, is an enzyme that synthesizes RNA from a DNA template. RNAP locally opens the double-stranded DNA (usually about four turns of the double helix) so that one strand of the exposed nucleotides can be used as a template for the synthesis of RNA, a .
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Genre/Form: Conference papers and proceedings Congresses: Additional Physical Format: Online version: Inhibitors of DNA and RNA polymerases. Oxford ; New York:. Parker, in Encyclopedia of Genetics, Bacterial RNA Polymerases. Bacteria have a single cellular RNA polymerase (RNAP), whose ‘holoenzyme’ form has five subunits: two copies of the relatively small α-subunit (each about 36 kDa), one copy each of large β- and β′-subunits ( kDa and kDa, respectively), and one copy of the σ-subunit, also called the ‘sigma factor.’.
Transcription is the first of several steps of DNA based gene expression in which a particular segment of DNA is copied into RNA (especially mRNA) by the enzyme RNA polymerase.
Both DNA and RNA are nucleic acids, which use base pairs of nucleotides as a complementary language. During transcription, a DNA sequence is read by an RNA polymerase, which produces a complementary, antiparallel RNA.
Bacteriophage T7 lysozyme is known to inhibit transcription by T7 RNA polymerase. Lysozyme present before initiation inhibited the synthesis of long RNA chains but did not inhibit elongation when added shortly after chains were initiated.
A combination of Cited by: Favipiravir (T; 6-fluorohydroxypyrazinecarboxamide) is an anti-viral agent that selectively and potently inhibits the RNA-dependent RNA polymerase (RdRp) of RNA viruses. Favipiravir was discovered through screening chemical library for anti-viral activity against the influenza virus by Toy Cited by: In this chapter the antibiotics are subdivided into those interacting with RNA polymerase from prokaryotic cells, and those interacting with RNA polymerases from eukaryotic organisms.
The short introductory survey on prokaryotic and eukaryotic RNA polymerases is based on the reviews of BURGESS (), BLATTI et al. () and KEDINGER et al. The inhibition by the flavonoids was due to competition with the template-primer in the case of the DNA polymerases, whereas the inhibition was due to competition with the triphosphate substrate (GTP) in the case of RNA polymerase.
The K 1 values of these flavonoid inhibitors for DNA and RNA polymerases was determined. Capacity of Nine Thermostable DNA Polymerases To Mediate DNA Amplification in the Presence of PCR-Inhibiting Samples.
Applied and Environmental Microbiology64 (10). DNA polymerases are unidirectional and can only elongate DNA chains in a 5' to 3' direction. A unique feature of some of these enzymes is their 'proofreading' ability. DNA polymerases I, II and III have 3' to 5' exonuclease activity and they can.
The span of viability of a cell characterized by the capacity to perform certain functions such as metabolism, growth, reproduction, some form of | Explore the latest full-text research PDFs. Enzymes that catalyze DNA template-directed extension of the 3'-end of an RNA strand one nucleotide at a time.
They can initiate a chain de novo. | Explore the. Hyone-Myong Eun, in Enzymology Primer for Recombinant DNA Technology, ii. Nucleotide sequencing. Reverse transcriptases (both AMV and MoLV) complement DNA-dependent DNA polymerases (e.g., Pol Ik) in the dideoxynucleotide sequencing of DNA, especially at the regions of high GC content and/or secondary structures ().Reverse transcriptase has been shown.
BET inhibitors cause promoter-proximal pausing of RNA polymerases. Early studies identified acute myeloid leukemia as especially sensitive to inhibitors of BET family members and the t(8;21) cell line Kasumi-1 appeared to be the most sensitive cell line (Zuber et al., ).We extended these results to the t(8;21)-containing SKNO-1 cell line that requires.
PCR inhibitors are any factor which prevent the amplification of nucleic acids through the polymerase chain reaction (PCR). PCR inhibition is the most common cause of amplification failure when sufficient copies of DNA are present.
PCR inhibitors usually affect PCR through interaction with DNA or interference with the DNA tors can escape removal during the DNA. Actinomycin D intercalates DNA and blocks the elongation of RNA polymerases (Sobell, ) as well as interferes with DNA topoisomerase I and II. Hepatitis C Virus NS5B RNA-Dependent RNA Polymerase: An Integral Part of HCV Antiviral Therapy 9.
HBV Polymerase as a Target for Development of Anti-HBV Drugs Polymerases of Coronaviruses: Structure, Function and Inhibitors Rhinovirus RNA Polymerase: Structure, Function, and Inhibitors Herpes Virus Polymerase Inhibitors This book represents the proceedings of the NATO Advanced Study Institute held in Santa Flavia, Sicily from the 20 - 29th June, In addition to the review talks given by the Lecturers at the Inst Control of DNA Replication in Bacteria.
Pritchard. Pages a. The genes and encoded proteins for the subunits of the yeast RNA polymerases have been isolated and the sequences determined, and some functional analysis has been done. Some of the subunits are homologous to bacterial RNA polymerases: The largest two subunits are homologs of b and b'.
The roughly 40 kDa subunit is the homolog of a. The clinically useful rifamycins include rifampin (known in some countries as rifampicin), a semisynthetic derivative of rifamycin B.
Rifamycin B and structurally related antibiotics inhibit bacterial RNA synthesis by binding to the β-subunit of bacterial DNA-dependent RNA polymerases.
A section of the chapter provides an overview of transcription in bacteria and. Inhibition of DNA repair enzymes tyrosyl-DNA phosphodiesterase 1 and poly(ADP-ribose)polymerases 1 and 2 in the presence of pyrimidine nucleoside derivatives was studied here.
New effective Tdp1 inhibitors were found in a series of nucleoside derivatives possessing 2′,3′,5′-tri-O-benzoyl-d-ribofuranose and 5-substituted uracil moieties and have half-maximal. Nuclei arc prepared from cells, sensitive or resistant to daunorubicin.
RNA polymerases A and B have an absolute requirement of divalent cations for activity. Native DNAs are better templates than heat‐denatured DNAs for RNA polymerase A. On the contrary heat‐denatured DNA is more transcribed than the native one by RNA polymerase B.6-Mercaptopurine ribonucleoside 5'-triphosphate was found to be an inhibitor of DNA-dependent RNA polymerases from Escherichia coli and chicken myeloblastosis cells.
The inhibitor appears to compete with GTP for its binding to RNA polymerase, resulting in a reduction of RNA chain initiations. Neither 6-mercaptopurine ribonucleoside nor its monophosphate derivative caused the inhibition.
Not only are there more control elements, there are also more RNA polymerases, which serve different specific cellular functions. Obviously, the broad function and location of all the RNA polymerases is the same: read a DNA template and transcribe an RNA copy of it; and since the DNA is found only in the nucleus, so are the polymerases.