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Gene Review

RPB11  -  DNA-directed RNA polymerase II core...

Saccharomyces cerevisiae S288c

Synonyms: B13.6, DNA-directed RNA polymerase II 13.6 kDa polypeptide, DNA-directed RNA polymerase II subunit RPB11, RNA polymerase II subunit B11, YOL005C
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High impact information on RPB11

  • Sequence alignments, combined with secondary-structure predictions, support proposals that a heterodimer of the eukaryotic RNAP subunits related to Saccharomyces cerevisiae Rpb3 and Rpb11 plays the role of the alphaNTD dimer in prokaryotic RNAP [1].
  • D also interacts under the same conditions with the RPB11 and AC19 subunits from the yeast Saccharomyces cerevisiae, suggesting that essential elements of the binding surface between these proteins have been conserved across the archaeal/eukaryotic evolutionary domain boundary [2].
  • Instead, allele-specific PCR, combined with GenBank database searches, suggests that a recent gene duplication event has resulted in distinct loci encoding three variant forms of RPB11 [3].
  • Association of RPB11 with SATB1 maps between amino acids 58 and 222 of SATB1, a region that includes a PDZ-like dimerization motif [3].
  • Northern blot analysis of normal tissues detected a particularly high expression of RPB11 mRNA in heart and skeletal muscle [4].

Biological context of RPB11

  • We report here the isolation and characterization of the yeast RNA polymerase II subunit RPB11, which is encoded by a single copy RPB11 gene located directly upstream of the topoisomerase I gene, TOPI, on chromosome XV [5].
  • In the case of Rpb3, growth was restored by increasing the gene dosage of the host Rpb11 or Rpb10 subunits, confirming previous evidence of a close genetic interaction between these three subunits [6].

Associations of RPB11 with chemical compounds

  • Determination of the precise orientation of the RNAPII in the holoenzyme indicates that Mediator contacts are centered on the RNAPII Rpb3/Rpb11 heterodimer, the eukaryotic homolog of the alpha(2) homodimer involved in transcription regulation in prokaryotes [7].

Other interactions of RPB11

  • We have sequenced two different cDNAs (AtRPB36a and AtRPB36b), the two corresponding genes from Arabidopsis thaliana that are homologs of yeast RPB3, and an Arabidopsis cDNA (AtRPB13.6) that is a homolog of yeast RPB11 [8].
  • As the isolation of RPB11 completes the isolation of known yeast RNA polymerase II subunit genes, we briefly summarize the salient features of these twelve genes and the polypeptides that they encode [5].


  1. Structure of the Escherichia coli RNA polymerase alpha subunit amino-terminal domain. Zhang, G., Darst, S.A. Science (1998) [Pubmed]
  2. In vitro assembly of an archaeal D-L-N RNA polymerase subunit complex reveals a eukaryote-like structural arrangement. Eloranta, J.J., Kato, A., Teng, M.S., Weinzierl, R.O. Nucleic Acids Res. (1998) [Pubmed]
  3. The thymocyte-specific MAR binding protein, SATB1, interacts in vitro with a novel variant of DNA-directed RNA polymerase II, subunit 11. Durrin, L.K., Krontiris, T.G. Genomics (2002) [Pubmed]
  4. Cloning of a novel human RNA polymerase II subunit downregulated by doxorubicin: new potential mechanisms of drug related toxicity. Fanciulli, M., Bruno, T., Cerboni, C., Bonetto, F., Iacobini, C., Frati, L., Piccoli, M., Floridi, A., Santoni, A., Punturieri, A. FEBS Lett. (1996) [Pubmed]
  5. Yeast RNA polymerase II subunit RPB11 is related to a subunit shared by RNA polymerase I and III. Woychik, N.A., McKune, K., Lane, W.S., Young, R.A. Gene Expr. (1993) [Pubmed]
  6. Functional conservation of RNA polymerase II in fission and budding yeasts. Shpakovski, G.V., Gadal, O., Labarre-Mariotte, S., Lebedenko, E.N., Miklos, I., Sakurai, H., Proshkin, S.A., Van Mullem, V., Ishihama, A., Thuriaux, P. J. Mol. Biol. (2000) [Pubmed]
  7. Structure of the yeast RNA polymerase II holoenzyme: Mediator conformation and polymerase interaction. Davis, J.A., Takagi, Y., Kornberg, R.D., Asturias, F.A. Mol. Cell (2002) [Pubmed]
  8. Association between 36- and 13.6-kDa alpha-like subunits of Arabidopsis thaliana RNA polymerase II. Ulmasov, T., Larkin, R.M., Guilfoyle, T.J. J. Biol. Chem. (1996) [Pubmed]
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