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RpII215  -  RNA polymerase II 215kD subunit

Drosophila melanogaster

Synonyms: 8WG16, CG1554, CTD, DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerase III largest subunit, ...
 
 
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Disease relevance of RpII215

  • Segments of the amino acid sequence predicted by the only long open reading frame of the RpII215 gene transcript display striking homology with corresponding segments of the beta subunit of E. coli RNA polymerase [1].
  • In general, our phage display method is faster, easier, and cheaper than the construction of overlapping fusion proteins or the use of synthetic peptides, especially in cases where the antigen is a large polypeptide such as the 215 kDa subunit of eukaryotic RNA polymerase II [2].
  • Using previously cloned P element sequences as a hybridization probe we have isolated a hybrid lambda phage clone carrying a 10 kb genomic DNA fragment containing a 1.3 kb P element insert and flanking sequences from the RpII locus [3].
  • The adenovirus EIA and pseudorabies virus immediate early (IE) proteins induce transcription from transfected viral and nonviral genes transcribed by RNA polymerase II (class II genes) [4].
  • The predicted amino acid sequence of the vaccinia 147-kDa subunit shows extensive homology with the largest subunit of Escherichia coli RNA polymerase, yeast RNA polymerases II and III, and Drosophila RNA polymerase II [5].
 

High impact information on RpII215

  • H3.3 replacement occurred prominently at sites of abundant RNA polymerase II and methylated H3 Lys4 throughout the genome and was enhanced on the dosage-compensated male X chromosome [6].
  • Protein-DNA cross-linking of cultured Drosophila cells has shown that, in vivo, prior to the induction of heat shock, there is approximately one molecule of RNA polymerase II associated with the promoter region of the major heat shock gene, hsp70 [7].
  • As demonstrated here, two polyadenylated jockey transcripts detected at different stages of Drosophila ontogenesis and in cell cultures have the same length as genomic copies of jockey and correspond to the strand containing ORFs. alpha-amanitin experiments indicate that jockey is transcribed by RNA polymerase II [8].
  • Like RNA polymerase II, topoisomerase I is recruited to heat-shock genes during the heat-shock response [9].
  • The non-P sequences in this clone (lambda DmRpII-1) hybridize to polytene chromosome band region 10C, the cytogenetic location of RpIIC4, and revertants which lose the lethal RNA polymerase II mutation also lose P element sequences from the locus [3].
 

Chemical compound and disease context of RpII215

 

Biological context of RpII215

  • DNA sequence analysis of RpII215, the gene that encodes the Mr215,000 subunit of RNA polymerase II (EC 2.7.7.6) in Drosophila melanogaster, reveals that the 3'-terminal exon includes a region encoding a C-terminal domain composed of 42 repeats of a seven-residue amino acid consensus sequence, Tyr-Ser-Pro-Thr-Ser-Pro-Ser [11].
  • We have mapped a number of mutations at the DNA sequence level in genes encoding the largest (RpII215) and second-largest (RpII140) subunits of Drosophila melanogaster RNA polymerase II [12].
  • Nucleotide variation in an 8.1-kb fragment encompassing the RpII215 gene, which encodes the largest subunit of the RNA polymerase II complex, is analyzed in a sample of 11 chromosomes from a natural population of Drosophila subobscura [13].
  • Another mutant phenotype is caused by certain RpII215 alleles, including all class I alleles [14].
  • Two mutations in the gene, RpII215, were analyzed to determine their effects on cell differentiation and proliferation [15].
 

Anatomical context of RpII215

  • Using a cell-free system to reconstitute chromatin with increased histone acetylation levels, we directly tested for a causal role of histone acetylation in transcription by RNA pol II [16].
  • Thus, even in the presence of known transcriptional activators, RNAP II dependent gene expression is actively repressed in early germ cells [17].
  • Our results indicate that p255 represents a highly phosphorylated form of RNA polymerase II largest subunit physically associated with spliceosomes and possibly involved in coupling transcription to RNA processing [18].
  • In mouse and Drosophila cultured cells the electrophoretic mobility of p255, faster in the latter species, was identical to that of the hyperphosphorylated form of RNA polymerase II largest subunit (IIo) [18].
  • The nuclear matrix protein p255 is a highly phosphorylated form of RNA polymerase II largest subunit which associates with spliceosomes [18].
 

Associations of RpII215 with chemical compounds

  • Class I alleles, including Ubl, C4, C11, JH1, and WJK2, enhance Ubx when heterozygous with class II alleles, which include wild-type RpII215 [14].
  • Surprisingly, the density of transcribing Pol II and Pol II progression through hsp70 in vivo are nearly normal in flavopiridol-treated cells [19].
  • In addition, mutational analyses revealed that several tryptophan residues in MTAD are important for the interaction with Pol II and transactivation [20].
  • Twenty one percent of the iDNA clones that have detectable transcriptionally engaged Pol II appear to be paused, in that they display sarkosyl-stimulated trancription in a nuclear run-on transcription assay [21].
  • Lastly, the recovery of RNA polymerase II largest subunit from HeLa splicing mixtures was compromised by EDTA, which prevents the interaction of p255 with splicing complexes and inhibits splicing [18].
 

Physical interactions of RpII215

  • Ubl displays a complex series of interactions with loci other than Ubx and elicits expression of specific mutant phenotypes when it is heterozygous in trans with certain nonallelic deficiencies and recessive mutations [22].
 

Enzymatic interactions of RpII215

  • As the kinase subunit of TFIIH, Cdk7 participates in basal transcription by phosphorylating the carboxy-terminal domain of the largest subunit of RNA polymerase II [23].
 

Regulatory relationships of RpII215

 

Other interactions of RpII215

 

Analytical, diagnostic and therapeutic context of RpII215

References

  1. Structure of the eukaryotic transcription apparatus: features of the gene for the largest subunit of Drosophila RNA polymerase II. Biggs, J., Searles, L.L., Greenleaf, A.L. Cell (1985) [Pubmed]
  2. Mapping of linear epitopes recognized by monoclonal antibodies with gene-fragment phage display libraries. Petersen, G., Song, D., Hügle-Dörr, B., Oldenburg, I., Bautz, E.K. Mol. Gen. Genet. (1995) [Pubmed]
  3. Molecular cloning of sequences from a Drosophila RNA polymerase II locus by P element transposon tagging. Searles, L.L., Jokerst, R.S., Bingham, P.M., Voelker, R.A., Greenleaf, A.L. Cell (1982) [Pubmed]
  4. Transcription of class III genes activated by viral immediate early proteins. Gaynor, R.B., Feldman, L.T., Berk, A.J. Science (1985) [Pubmed]
  5. Homology between RNA polymerases of poxviruses, prokaryotes, and eukaryotes: nucleotide sequence and transcriptional analysis of vaccinia virus genes encoding 147-kDa and 22-kDa subunits. Broyles, S.S., Moss, B. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  6. Genome-scale profiling of histone H3.3 replacement patterns. Mito, Y., Henikoff, J.G., Henikoff, S. Nat. Genet. (2005) [Pubmed]
  7. The RNA polymerase II molecule at the 5' end of the uninduced hsp70 gene of D. melanogaster is transcriptionally engaged. Rougvie, A.E., Lis, J.T. Cell (1988) [Pubmed]
  8. jockey, a mobile Drosophila element similar to mammalian LINEs, is transcribed from the internal promoter by RNA polymerase II. Mizrokhi, L.J., Georgieva, S.G., Ilyin, Y.V. Cell (1988) [Pubmed]
  9. Topoisomerase I interacts with transcribed regions in Drosophila cells. Gilmour, D.S., Pflugfelder, G., Wang, J.C., Lis, J.T. Cell (1986) [Pubmed]
  10. Characterization of RNA polymerase II-dependent transcription in Xenopus extracts. Toyoda, T., Wolffe, A.P. Dev. Biol. (1992) [Pubmed]
  11. The C-terminal repeat domain of RNA polymerase II largest subunit is essential in vivo but is not required for accurate transcription initiation in vitro. Zehring, W.A., Lee, J.M., Weeks, J.R., Jokerst, R.S., Greenleaf, A.L. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  12. Mapping mutations in genes encoding the two large subunits of Drosophila RNA polymerase II defines domains essential for basic transcription functions and for proper expression of developmental genes. Chen, Y., Weeks, J., Mortin, M.A., Greenleaf, A.L. Mol. Cell. Biol. (1993) [Pubmed]
  13. Nucleotide polymorphism at the RpII215 gene in Drosophila subobscura. Weak selection on synonymous mutations. Llopart, A., Aguadé, M. Genetics (2000) [Pubmed]
  14. Antagonistic interactions between alleles of the RpII215 locus in Drosophila melanogaster. Mortin, M.A., Kim, W.J., Huang, J. Genetics (1988) [Pubmed]
  15. Clonal analysis of two mutations in the large subunit of RNA polymerase II of Drosophila. Mortin, M.A., Perrimon, N., Bonner, J.J. Mol. Gen. Genet. (1985) [Pubmed]
  16. Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin. Nightingale, K.P., Wellinger, R.E., Sogo, J.M., Becker, P.B. EMBO J. (1998) [Pubmed]
  17. Regulation of zygotic gene expression in Drosophila primordial germ cells. Van Doren, M., Williamson, A.L., Lehmann, R. Curr. Biol. (1998) [Pubmed]
  18. The nuclear matrix protein p255 is a highly phosphorylated form of RNA polymerase II largest subunit which associates with spliceosomes. Vincent, M., Lauriault, P., Dubois, M.F., Lavoie, S., Bensaude, O., Chabot, B. Nucleic Acids Res. (1996) [Pubmed]
  19. Coordination of transcription, RNA processing, and surveillance by P-TEFb kinase on heat shock genes. Ni, Z., Schwartz, B.E., Werner, J., Suarez, J.R., Lis, J.T. Mol. Cell (2004) [Pubmed]
  20. Dual roles of RNA helicase A in CREB-dependent transcription. Aratani, S., Fujii, R., Oishi, T., Fujita, H., Amano, T., Ohshima, T., Hagiwara, M., Fukamizu, A., Nakajima, T. Mol. Cell. Biol. (2001) [Pubmed]
  21. Direct cloning of DNA that interacts in vivo with a specific protein: application to RNA polymerase II and sites of pausing in Drosophila. Law, A., Hirayoshi, K., O'Brien, T., Lis, J.T. Nucleic Acids Res. (1998) [Pubmed]
  22. An RNA polymerase II mutation in Drosophila melanogaster that mimics ultrabithorax. Mortin, M.A., Lefevre, G. Chromosoma (1981) [Pubmed]
  23. Xpd/Ercc2 regulates CAK activity and mitotic progression. Chen, J., Larochelle, S., Li, X., Suter, B. Nature (2003) [Pubmed]
  24. Drosophila RNA polymerase II elongation factor DmS-II has homology to mouse S-II and sequence similarity to yeast PPR2. Marshall, T.K., Guo, H., Price, D.H. Nucleic Acids Res. (1990) [Pubmed]
  25. The carboxyl-terminal repeat domain of RNA polymerase II is not required for transcription factor Sp1 to function in vitro. Zehring, W.A., Greenleaf, A.L. J. Biol. Chem. (1990) [Pubmed]
  26. The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila. Andrulis, E.D., Werner, J., Nazarian, A., Erdjument-Bromage, H., Tempst, P., Lis, J.T. Nature (2002) [Pubmed]
  27. DNA Binding Properties of TAF1 Isoforms with Two AT-hooks. Metcalf, C.E., Wassarman, D.A. J. Biol. Chem. (2006) [Pubmed]
  28. Increased UV light sensitivity in transgenic Drosophila expressing the antisense XPD homolog. Sandoval, M.T., Zurita, M. Antisense Nucleic Acid Drug Dev. (2001) [Pubmed]
  29. The Drosophila RNA-binding protein RBP1 is localized to transcriptionally active sites of chromosomes and shows a functional similarity to human splicing factor ASF/SF2. Kim, Y.J., Zuo, P., Manley, J.L., Baker, B.S. Genes Dev. (1992) [Pubmed]
  30. Cloning and sequence analysis of the mouse genomic locus encoding the largest subunit of RNA polymerase II. Ahearn, J.M., Bartolomei, M.S., West, M.L., Cisek, L.J., Corden, J.L. J. Biol. Chem. (1987) [Pubmed]
  31. Purification and immunological analysis of RNA polymerase II from Caenorhabditis elegans. Sanford, T., Prenger, J.P., Golomb, M. J. Biol. Chem. (1985) [Pubmed]
 
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