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P-TEFb mediates a transition into productive elongation by phosphorylating the two negative factors and the polymerase and is regulated by association with the 7SK snRNP. The positive transcription elongation factor, P-TEFb , is a multiprotein complex that plays an essential role in the regulation of transcription by RNA polymerase II (Pol II ...
Cell division is the process by which a parent cell divides into two daughter cells. [1] Cell division usually occurs as part of a larger cell cycle in which the cell grows and replicates its chromosome(s) before dividing.
Structure of Taq DNA polymerase. In biochemistry, a polymerase is an enzyme (EC 2.7.7.6/7/19/48/49) that synthesizes long chains of polymers or nucleic acids. DNA polymerase and RNA polymerase are used to assemble DNA and RNA molecules, respectively, by copying a DNA template strand using base-pairing interactions or RNA by half ladder replication.
FACT (facilitates chromatin transcription, [1] sometimes facilitates chromatin transactions [2] [3]) is a heterodimeric protein complex that affects eukaryotic RNA polymerase II (Pol II) transcription elongation both in vitro and in vivo.
DNA polymerase's rapid catalysis due to its processive nature. Processivity is a characteristic of enzymes that function on polymeric substrates. In the case of DNA polymerase, the degree of processivity refers to the average number of nucleotides added each time the enzyme binds a template.
The cell cycle is a series of complex, ordered, sequential events that control how a single cell divides into two cells, and involves several different phases. The phases include the G1 and G2 phases, DNA replication or S phase, and the actual process of cell division, mitosis or M phase. [1]
MCM2-7 is required for both DNA replication initiation and elongation; its regulation at each stage is a central feature of eukaryotic DNA replication. [3] During G1 phase, the two head-to-head Mcm2-7 rings serve as the scaffold for the assembly of the bidirectional replication initiation complexes at the replication origin.
These explain how T7 polymerase binds to DNA and transcribes it. The N-terminal domain moves around as the elongation complex forms. The ssRNAP holds a DNA-RNA hybrid of 8bp. [3] A beta-hairpin specificity loop (residues 739-770 in T7) recognizes the promoter; swapping it out for one found in T3 RNAP makes the polymerase recognize T3 promoters ...