RNA polymerase II, Pol II, RNAPII, PolII, CTD
large subunit of the enzyme that catalyzes the synthesis of a complementary strand of RNA from a DNA template - context-dependent conformational switches and biased dephosphorylation suggest a mechanism for the selective recruitment of cis-proline-specific regulatory factors and region-specific modulation of the C-terminal domain code that may augment gene regulation
Gene model reviewed during 5.50
There is only one protein coding transcript and one polypeptide associated with this gene
Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits.
The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatase, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed.
The C-terminal domain (CTD) serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\RpII215 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\RpII215 in GBrowse 2
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
Source for identity of: RpII215 CG1554
Source for merge of: l(1)G0040 RpII215
Most alleles are recessive lethals. All enhance expression of Ubx in RpII215/+ heterozygotes with the effect of + (no effect) < RpII215H1 < RpII2157 < RpII215K2 < RpII2154 < RpII215Ubl. Heteroallelic combinations of these mutants produce either a reduced effect when RpII215Ubl is involved or no effect in other combinations.
In a sample of 79 genes with multiple introns, 33 showed significant heterogeneity in G+C content among introns of the same gene and significant positive correspondence between the intron and the third codon position G+C content within genes. These results are consistent with selection adding against preferred codons at the start of genes.
Suppressor mutations isolated on the basis of restoring viability to RpII215 and RpII140 mutants identify discrete domains in either subunit. The mutations recovered are not random and might provide insights into possible mechanisms for mutagenesis in eukaryotes.
Used in a phylogenetic analysis, the tree in inferred by parsimony method from RpoB sequences, or homologous, multiple alignment.
Hsf interacts directly with the general transcription factor Tbp and these two factor bind cooperatively to heat shock promoters. The acidic domain of RpII215 associates with Tbp in vitro and is specifically displaced from Tbp upon addition of Hsf.
An assay for the phosphorylation of RNA polymerase II by CTD-kinases has been developed and the localisation on polytene chromosomes of the phosphorylated (PolII0) and nonphosphorylated (PolIIA) forms of the enzyme compared.
The distribution of different isoforms of the large subunit of RNA polymerase II (encoded by RpII215) in Drosophila embryos has been analysed.
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.
Removal of the carboxy terminal domain (CTD) of the large subunit of RNA polymerase II (RpII215) abolished productive elongation. Cdk9 can phosphorylate the CTD and this phosphorylation controls the transition from abortive into productive elongation mode.
Removal of the entire CTD repeats renders RpII215 completely defective in vivo, whereas eliminating half of the CTD results in a polymerase with significant in vivo activity.
RNA polymerase II is well suited for the elucidation of the evolutionary relationships among eukaryotes.
The technique of paramagnetic particle-mediated selection of terminated run-on transcripts was used to examine RNA polymerase II pausing and 5' cap formation at high resolution on the heat shock genes Hsp70A, Hsp70B, Hsp26 and Hsp27. Results demonstrate that polymerases pause over a narrow region of each heat shock gene, not at a defined point. 5' capping occurs over a region coincidental with that of pausing.
Protein complexes of RNA polymerase II localise to major developmental puffs and heat shock puffs.
Mutations in zygotic gene RpII215 do not interact with RpII140wimp.
The protein coding sequences and the 5' end of RpII215 have been located by sequencing 2582 bases of DNA from coordinates +0.4 to -2.18.
P element reversion gives rise to different revertants that retain different levels of gene function.
The structural gene encoding the 215kD subunit of RNA polymerase II (RNA nucleotidyl transferase. This subunit highly conserved as inferred from the cross-reaction of antiserum from the large subunit of calf RNA polymerase II with enzyme isolated from Drosophila as well as that from yeast and wheat germ (Carrol and Stollar, 1983); also amino-acid sequence homology detected with the β' subunit of E.coli RNA polymerase (Biggs, Searles, and Greenleaf, 1985). Dosage compensated at the level of transcription (Faust, Renkawitz-Pohl, Falkenburg, Gasch, Bialojan, Young and Bautz, 1986).