Disease relevance of RpII15

• The human immunodeficiency virus transactivator protein, Tat, provides the first example of the regulation of viral gene expression through control of elongation by RNA polymerase II [1].

High impact information on RpII15

• The transition from abortive into productive elongation is proposed to be controlled by a positive transcription elongation factor b (P-TEFb) through phosphorylation of the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II [2].
• We show that Pcf11 is directly involved in termination in Drosophila. dPcf11 is concentrated at the 3' end of the hsp70 gene in cells, and depletion of dPcf11 with RNAi causes Pol II to readthrough the normal region of termination. dPcf11 also localizes to most transcribed loci on polytene chromosomes [3].
• Unlike the TAFs and Pol II, the interaction between Mediator and HSF on chromosomal loci is direct and mechanistically separable from the preinitiation complex assembly step [4].
• Here, we show that upon heat shock the Pol II-free form of Mediator is rapidly recruited to HSF binding sites [4].
• These data suggest that the chromatin remodeling activity of the BRM complex plays a general role in facilitating transcription by RNA polymerase II [5].

Biological context of RpII15

• An 800-bp 5' enhancer was identified that recapitulates this complex pattern when attached to a RNA polymerase II core promoter fused to a lacZ-reporter gene [6].
• In this model, Ess1 binds and isomerizes the CTD of RNA polymerase II, thus altering its interaction with proteins required for transcription of essential cell cycle genes [7].
• Rtt109 Is Required for Proper H3K56 Acetylation: A CHROMATIN MARK ASSOCIATED WITH THE ELONGATING RNA POLYMERASE II [8].
• The multiprotein Mediator complex is a coactivator required for transcriptional activation of RNA polymerase II transcribed genes by DNA binding transcription factors [9].
• The kinetics of heat inactivation of RNA polymerase II in crude extracts could be reproducibly measured [10].

Anatomical context of RpII15

• In preparations of polytene chromosomes from salivary gland nuclei, SARFH antibodies recognize their target associated with the majority of active transcription units, revealed by colocalization with the phosphorylated form of RNA Pol II [11].

Associations of RpII15 with chemical compounds

• The ability of P-TEFb to phosphorylate the carboxyl-terminal domain of the large subunit of RNA polymerase II was inhibited by flavopiridol with a K(i) of 3 nm [12].
• The two forms of RNA polymerase II differ in ammonium sulfate optima [13].
• Thioether 2 and sulfoxide 3-R exert 50% inhibition of RNA polymerase II (or B) from Drosophila melanogaster in 10(-6) M solution whereas Ki of 3-S is about five times higher [14].

Other interactions of RpII15

• The PSE is essential for transcription of both RNA polymerase II-transcribed and RNA polymerase III-transcribed snRNA genes and is recognized in DROSOPHILA: by a multi-subunit protein factor termed DM:PBP [15].

Analytical, diagnostic and therapeutic context of RpII15

• Using the polymerase chain reaction the coding region of RPII15 was isolated from genomic DNA of adult flies [16].
• The chromatin immunoprecipitation assays revealed that HDI treatments induced the hyperacetylation of histone H3 at the promoter and the transcribing regions of hsp70 gene, increased the accessibility of heat-shock factor to target heat-shock element, and promoted the RNA polymerase II-mediated transcription [17].
• As judged by gel filtration chromatography, female adult extracts have forms of RNA polymerase II that differ in molecular weight and template preference [13].

References