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Gene Review

prd  -  paired

Drosophila melanogaster

Synonyms: CG6716, Dmel\CG6716, PRD, Prd, Segmentation protein paired, ...
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High impact information on prd

  • We show that changing a single amino acid at the C-terminus of the recognition helix is both necessary and sufficient to confer the DNA binding specificity of either Ftz or Bcd on Prd [1].
  • We investigated the nature of homeodomain-DNA interactions by making a series of mutations in the helix-turn-helix motif of the Drosophila homeodomain protein Paired (Prd) [1].
  • In addition to the prd-specific his-pro repeat, some of the 12 genes contain M-repeats and two new types of homeo boxes not detectable by hybridization with the two known classes of homeo boxes [2].
  • We show that cooperative dimerization on palindromic DNA sequences can provide increased specificity to one of the three major classes of homeo domains, the Paired/Pax class [3].
  • The cooperative dimerization of homeo domains in the Prd class distinguishes them from other classes, whereas binding-site configuration and sequence specificity allow for distinctions within this class [3].

Biological context of prd

  • Drosophila Paired regulates late even-skipped expression through a composite binding site for the paired domain and the homeodomain [4].
  • Transgenic analysis shows that this regulation is largely mediated by an evolutionarily conserved sequence within the late element termed PTE (Paired Target Element) [4].
  • Mutagenesis of either binding site leads to significant reduction in the activity of the late element, indicating that both DNA-binding domains in the Paired protein are required for regulation [4].
  • The organisation of the Prd-binding sites, as well as the necessity for intact DNA binding sites for both paired- and homeodomains, suggests a molecular model whereby the two DNA-binding domains of the Prd protein cooperate in transcriptional activation of gsb [5].
  • The transcription factor Paired (Prd) is the main activator of this enhancer in all parasegments of the embryo [5].

Anatomical context of prd

  • The model predicts the distributions of pair-rule gene products regulating prd at late syncytial blastoderm, e.g., that of opa [6].

Associations of prd with chemical compounds

  • They are characterized by six invariant amino acid residues in the homeodomain, while the residue at position 50 can be a serine, glutamine or lysine as in the Pax-type, Q50 Paired-like or the K50 Paired-like homeodomains respectively [7].

Regulatory relationships of prd

  • When ppa function was removed from cells that express prd mRNA, Prd protein levels increased [8].
  • The transition of the early 'pair-rule' to the 'segment-polarity' pattern of prd expression is regulated by the secondary pair-rule genes opa and odd [6].

Other interactions of prd

  • When ppa was expressed ectopically in these cells, Prd protein, but not mRNA, levels diminished [8].
  • In normal development, Prd functions only in cells in which ppa mRNA expression has been repressed by another segmentation protein, Even-skipped (Eve) [8].
  • This positive activity appears to be in competition with Eve and Ftz on Prd homeodomain-binding sites [5].
  • In Tribolium, homologs of almost all the eight canonical Drosophila pair-rule genes are expressed in pair-rule domains, but only five have pair-rule functions. even-skipped, runt and odd-skipped act as primary pair-rule genes, while the functions of paired (prd) and sloppy-paired (slp) are secondary [9].
  • The temporal profiles of BSH9 and BSH4 transcripts, as characterized by Northern analysis, show a peak shortly after the peak of prd transcripts [10].

Analytical, diagnostic and therapeutic context of prd

  • Using site-directed mutagenesis, we have identified sites critical for Prd activity [5].
  • Structure-based sequence alignment and molecular modeling in conjunction with mutational analysis suggest that the HTH motif is part of a three-helix bundle, with remarkable similarity to paired (prd), a developmental regulatory protein from Drosophila [11].


  1. A single amino acid can determine the DNA binding specificity of homeodomain proteins. Treisman, J., Gönczy, P., Vashishtha, M., Harris, E., Desplan, C. Cell (1989) [Pubmed]
  2. Structure of the segmentation gene paired and the Drosophila PRD gene set as part of a gene network. Frigerio, G., Burri, M., Bopp, D., Baumgartner, S., Noll, M. Cell (1986) [Pubmed]
  3. Cooperative dimerization of paired class homeo domains on DNA. Wilson, D., Sheng, G., Lecuit, T., Dostatni, N., Desplan, C. Genes Dev. (1993) [Pubmed]
  4. Drosophila Paired regulates late even-skipped expression through a composite binding site for the paired domain and the homeodomain. Fujioka, M., Miskiewicz, P., Raj, L., Gulledge, A.A., Weir, M., Goto, T. Development (1996) [Pubmed]
  5. Combinatorial activity of pair-rule proteins on the Drosophila gooseberry early enhancer. Bouchard, M., St-Amand, J., Côté, S. Dev. Biol. (2000) [Pubmed]
  6. Network of interactions among pair-rule genes regulating paired expression during primordial segmentation of Drosophila. Baumgartner, S., Noll, M. Mech. Dev. (1990) [Pubmed]
  7. Evolution of homeobox genes: Q50 Paired-like genes founded the Paired class. Galliot, B., de Vargas, C., Miller, D. Dev. Genes Evol. (1999) [Pubmed]
  8. Targeted localized degradation of Paired protein in Drosophila development. Raj, L., Vivekanand, P., Das, T.K., Badam, E., Fernandes, M., Finley, R.L., Brent, R., Appel, L.F., Hanes, S.D., Weir, M. Curr. Biol. (2000) [Pubmed]
  9. Evolutionary flexibility of pair-rule patterning revealed by functional analysis of secondary pair-rule genes, paired and sloppy-paired in the short-germ insect, Tribolium castaneum. Choe, C.P., Brown, S.J. Dev. Biol. (2007) [Pubmed]
  10. Structure of two genes at the gooseberry locus related to the paired gene and their spatial expression during Drosophila embryogenesis. Baumgartner, S., Bopp, D., Burri, M., Noll, M. Genes Dev. (1987) [Pubmed]
  11. Identification of the domains for DNA binding and transactivation function of C protein from bacteriophage Mu. Paul, B.D., Kanhere, A., Chakraborty, A., Bansal, M., Nagaraja, V. Proteins (2003) [Pubmed]
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