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Gene Review

Rpd3  -  CG7471 gene product from transcript CG7471-RA

Drosophila melanogaster

Synonyms: CG7471, DHDAC1, DRpd3, DmHDAC1, Dmel\CG7471, ...
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Disease relevance of Rpd3

  • In addition, we found that the transcriptional repressor protein, lethal (3) malignant brain tumor protein, L(3)MBT, and the histone deacetylase, Rpd3, associated with the Myb-MuvB complex [1].

Psychiatry related information on Rpd3

  • These findings raise the possibility that therapy with HDAC inhibitors may slow or prevent the progressive neurodegeneration seen in Huntington's disease and other polyglutamine-repeat diseases, even after the onset of symptoms [2].

High impact information on Rpd3


Biological context of Rpd3

  • Finally, we found that a heterozygous deficiency for the histone deacetylase, Rpd3, masked the radiation-resistant phenotype of both esc and E(Pc) mutants [6].
  • PCL and E(Z) colocalize virtually completely on polytene chromosomes and are associated with a subset of RPD3 sites [7].
  • We show that RPD3 is required for silencing mediated by a Polycomb response element (PRE) in vivo and that E(Z) and RPD3 are bound to the Ubx PRE in vivo, suggesting that they act directly at the PRE [8].
  • We show that Drosophila Hdac1, an Rpd3-type gene, interacts cooperatively with Polycomb group repressors in silencing the homeotic genes that are essential for axial patterning of body segments [9].
  • Loss of RPD3 reduces the growth rate of cells but does not cause a distinct cell cycle defect, suggesting that cells are delayed in multiple phases of the cell cycle, including G(2) [10].

Associations of Rpd3 with chemical compounds


Physical interactions of Rpd3

  • Here we show that the SIN3/RPD3 complex and the corepressor SMRTER are required for Drosophila G(2) phase cell cycle progression [10].
  • Consistent with this, recombinant dHDAC1 coimmunoprecipitates with components of the Drosophila NuRD complex and dHDAC3 with an as yet unknown 45-kDa protein [14].
  • We suggest a model in which the concerted histone deacetylation and methylation by a SU(VAR)3-9/HDAC1-containing complex leads to a permanent silencing of transcription in particular areas of the genome [15].

Other interactions of Rpd3

  • The association of ESC and E(Z) with p55 and RPD3 is conserved in mammals [8].
  • Functional interaction between the Drosophila knirps short range transcriptional repressor and RPD3 histone deacetylase [16].
  • Two highly conserved histone deacetylases, Sir2 and Rpd3, have been linked to caloric restriction and the extension of longevity [17].
  • The relatively mild defects observed in Rpd3 mutants suggest that the recently identified Groucho and dCtBP corepressor proteins do not function solely through the recruitment of histone deacetylases [18].
  • Mutation of the histone deacetylase (HDAC) Rpd3 induced genome-wide hyperacetylation, genomic replication and a redistribution of the origin-binding protein ORC2 in amplification-stage cells, independent of effects on transcription [19].

Analytical, diagnostic and therapeutic context of Rpd3


  1. Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor complex. Lewis, P.W., Beall, E.L., Fleischer, T.C., Georlette, D., Link, A.J., Botchan, M.R. Genes Dev. (2004) [Pubmed]
  2. Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila. Steffan, J.S., Bodai, L., Pallos, J., Poelman, M., McCampbell, A., Apostol, B.L., Kazantsev, A., Schmidt, E., Zhu, Y.Z., Greenwald, M., Kurokawa, R., Housman, D.E., Jackson, G.R., Marsh, J.L., Thompson, L.M. Nature (2001) [Pubmed]
  3. Distinct in vivo requirements for establishment versus maintenance of transcriptional repression. Wheeler, J.C., VanderZwan, C., Xu, X., Swantek, D., Tracey, W.D., Gergen, J.P. Nat. Genet. (2002) [Pubmed]
  4. A functional interaction between the histone deacetylase Rpd3 and the corepressor groucho in Drosophila development. Chen, G., Fernandez, J., Mische, S., Courey, A.J. Genes Dev. (1999) [Pubmed]
  5. Downregulation of lipopolysaccharide response in Drosophila by negative crosstalk between the AP1 and NF-kappaB signaling modules. Kim, T., Yoon, J., Cho, H., Lee, W.B., Kim, J., Song, Y.H., Kim, S.N., Yoon, J.H., Kim-Ha, J., Kim, Y.J. Nat. Immunol. (2005) [Pubmed]
  6. Mutations in the extra sex combs and Enhancer of Polycomb Genes Increase Homologous Recombination in Somatic Cells of Drosophila melanogaster. Holmes, A.M., Weedmark, K.A., Gloor, G.B. Genetics (2006) [Pubmed]
  7. A 1-megadalton ESC/E(Z) complex from Drosophila that contains polycomblike and RPD3. Tie, F., Prasad-Sinha, J., Birve, A., Rasmuson-Lestander, A., Harte, P.J. Mol. Cell. Biol. (2003) [Pubmed]
  8. The Drosophila Polycomb Group proteins ESC and E(Z) are present in a complex containing the histone-binding protein p55 and the histone deacetylase RPD3. Tie, F., Furuyama, T., Prasad-Sinha, J., Jane, E., Harte, P.J. Development (2001) [Pubmed]
  9. Essential role of Drosophila Hdac1 in homeotic gene silencing. Chang, Y.L., Peng, Y.H., Pan, I.C., Sun, D.S., King, B., Huang, D.H. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  10. The SIN3/RPD3 deacetylase complex is essential for G(2) phase cell cycle progression and regulation of SMRTER corepressor levels. Pile, L.A., Schlag, E.M., Wassarman, D.A. Mol. Cell. Biol. (2002) [Pubmed]
  11. Biochemical analysis of transcriptional repression by Drosophila histone deacetylase 1. Huang, X., Kadonaga, J.T. J. Biol. Chem. (2001) [Pubmed]
  12. Groucho/TLE family proteins and transcriptional repression. Chen, G., Courey, A.J. Gene (2000) [Pubmed]
  13. Mutations at the Ser50 residue of translation factor eIF-2alpha dominantly affect developmental rate, body weight, and viability of Drosophila melanogaster. Qu, S., Perlaky, S.E., Organ, E.L., Crawford, D., Cavener, D.R. Gene Expr. (1997) [Pubmed]
  14. dSIR2 and dHDAC6: two novel, inhibitor-resistant deacetylases in Drosophila melanogaster. Barlow, A.L., van Drunen, C.M., Johnson, C.A., Tweedie, S., Bird, A., Turner, B.M. Exp. Cell Res. (2001) [Pubmed]
  15. Physical and functional association of SU(VAR)3-9 and HDAC1 in Drosophila. Czermin, B., Schotta, G., Hülsmann, B.B., Brehm, A., Becker, P.B., Reuter, G., Imhof, A. EMBO Rep. (2001) [Pubmed]
  16. Functional interaction between the Drosophila knirps short range transcriptional repressor and RPD3 histone deacetylase. Struffi, P., Arnosti, D.N. J. Biol. Chem. (2005) [Pubmed]
  17. Drosophila longevity is not affected by heterochromatin-mediated gene silencing. Frankel, S., Rogina, B. Aging Cell (2005) [Pubmed]
  18. The Rpd3 histone deacetylase is required for segmentation of the Drosophila embryo. Mannervik, M., Levine, M. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  19. Chromatin regulates origin activity in Drosophila follicle cells. Aggarwal, B.D., Calvi, B.R. Nature (2004) [Pubmed]
  20. Longevity regulation by Drosophila Rpd3 deacetylase and caloric restriction. Rogina, B., Helfand, S.L., Frankel, S. Science (2002) [Pubmed]
  21. Dissecting the biological functions of Drosophila histone deacetylases by RNA interference and transcriptional profiling. Foglietti, C., Filocamo, G., Cundari, E., De Rinaldis, E., Lahm, A., Cortese, R., Steinkühler, C. J. Biol. Chem. (2006) [Pubmed]
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