Updating the rna polymerase ctd

04-Jun-2017 14:56

An assay for the phosphorylation of RNA polymerase II by CTD-kinases has been developed and the localisation on polytene chromosomes of the phosphorylated (Pol II0) and nonphosphorylated (Pol IIA) forms of the enzyme compared.

The interaction between alleles in different classes of polymerase occurs even in the absence of transcription by the wild type polymerase and occurs prior to the elongation and/or translocation step that is blocked or slowed by α-amanitin.

genes, references, stocks) or controlled vocabulary terms (e.g. The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat.

Pol II is the central component of the basal RNA polymerase II transcription machinery.

At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II.

A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition.

Hsf interacts directly with the general transcription factor Tbp and these two factor bind cooperatively to heat shock promoters.

The acidic domain of Rp II215 associates with Tbp in vitro and is specifically displaced from Tbp upon addition of Hsf.

Pol II is the central component of the basal RNA polymerase II transcription machinery.

At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II.

A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition.

Hsf interacts directly with the general transcription factor Tbp and these two factor bind cooperatively to heat shock promoters.

The acidic domain of Rp II215 associates with Tbp in vitro and is specifically displaced from Tbp upon addition of Hsf.

This section lists c DNAs and ESTs that fall within the genomic extent of the gene model, which may include c DNAs and ESTs of genes within introns, or of overlapping genes.