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Phc1  -  polyhomeotic-like 1 (Drosophila)

Mus musculus

Synonyms: AW557034, Early development regulatory protein 1, Edr, Edr1, Mph1, ...
 
 
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Disease relevance of Phc1

 

High impact information on Phc1

  • Polycomb group gene rae28 is required for sustaining activity of hematopoietic stem cells [6].
  • Hematopoietic activity was impaired in the fetal liver of rae28-deficient animals (rae28-/-), as demonstrated by progressive reduction of hematopoietic progenitors of multilineages and poor expansion of colony forming units in spleen (CFU-S(12)) during embryonic development [6].
  • This is the first report to suggest that rae28 has a crucial role in sustaining the activity of HSCs to maintain hematopoiesis [6].
  • The genetic interactions further reveal the functional overlap between Phc2 and Phc1 and a strict dose-dependent requirement during A-P specification and embryonic survival [7].
  • These results indicate that the rae28 gene is involved in the regulation of Hox gene expression and segment specification during paraxial mesoderm and neural crest development [8].
 

Chemical compound and disease context of Phc1

 

Biological context of Phc1

  • The sequences of individual oligonucleotides included the following consensus sequences; 5'-ACCA-3', 5'-ACCCA-3', 5'-CTATCA-3' and 5'-TGCC-3'. The oligonucleotides including these consensus sequences were show to have significant affinity with the GST-RAE28 fusion protein [10].
  • In this study we synthesized the glutathione S transferase-RAE28 (GST-RAE28) fusion protein and examined sequence-specific DNA binding activity in the RAE28 protein by using the selected and amplified binding site method [10].
  • During maturation of oocytes, significant alterations of Rae28/Ph1 and Ring1B localization are concordant with configuration changes of the chromatin at the germinal vesicle stage of meiotic prophase [4].
  • Importantly, dissociation of Rae28/Ph1 and Ring1B from the chromatin temporally correlates with transcriptional arrest both in mitosis and meiosis [4].
  • The overall exon-intron organization suggested that three different Rae28 mRNAs are generated through alternative splicing [11].
 

Anatomical context of Phc1

 

Other interactions of Phc1

  • In this study, we examined the time course of Hoxb3 expression during late gastrulation and early segmentation of rae28-deficient mice [12].
  • Severe B-cell maturation arrest was observed in rae28-/- between pro- and pre-B lymphocyte stages [3].
  • In this study, we analyzed subcellular localization of Rae28/Ph1 and Ring1B by using newly generated monoclonal antibodies in mitotic somatic cells and meiotic mouse oocytes [4].
  • Gel filtration analysis of embryonic extracts indicates that RAE28, BMI1 and M33 exist in large multimeric complexes [13].
 

Analytical, diagnostic and therapeutic context of Phc1

References

  1. The Polycomb-group gene Rae28 sustains Nkx2.5/Csx expression and is essential for cardiac morphogenesis. Shirai, M., Osugi, T., Koga, H., Kaji, Y., Takimoto, E., Komuro, I., Hara, J., Miwa, T., Yamauchi-Takihara, K., Takihara, Y. J. Clin. Invest. (2002) [Pubmed]
  2. Overexpression of Polycomb-group gene rae28 in cardiomyocytes does not complement abnormal cardiac morphogenesis in mice lacking rae28 but causes dilated cardiomyopathy. Koga, H., Kaji, Y., Nishii, K., Shirai, M., Tomotsune, D., Osugi, T., Sawada, A., Kim, J.Y., Hara, J., Miwa, T., Yamauchi-Takihara, K., Shibata, Y., Takihara, Y. Lab. Invest. (2002) [Pubmed]
  3. Lack of the Polycomb-group gene rae28 causes maturation arrest at the early B-cell developmental stage. Tokimasa, S., Ohta, H., Sawada, A., Matsuda, Y., Kim, J.Y., Nishiguchi, S., Hara, J., Takihara, Y. Exp. Hematol. (2001) [Pubmed]
  4. Dissociation of mammalian Polycomb-group proteins, Ring1B and Rae28/Ph1, from the chromatin correlates with configuration changes of the chromatin in mitotic and meiotic prophase. Miyagishima, H., Isono, K., Fujimura, Y., Iyo, M., Takihara, Y., Masumoto, H., Vidal, M., Koseki, H. Histochem. Cell Biol. (2003) [Pubmed]
  5. The Drosophila Polycomb group gene Sex comb on midleg (Scm) encodes a zinc finger protein with similarity to polyhomeotic protein. Bornemann, D., Miller, E., Simon, J. Development (1996) [Pubmed]
  6. Polycomb group gene rae28 is required for sustaining activity of hematopoietic stem cells. Ohta, H., Sawada, A., Kim, J.Y., Tokimasa, S., Nishiguchi, S., Humphries, R.K., Hara, J., Takihara, Y. J. Exp. Med. (2002) [Pubmed]
  7. Mammalian polyhomeotic homologues Phc2 and Phc1 act in synergy to mediate polycomb repression of Hox genes. Isono, K., Fujimura, Y., Shinga, J., Yamaki, M., O-Wang, J., Takihara, Y., Murahashi, Y., Takada, Y., Mizutani-Koseki, Y., Koseki, H. Mol. Cell. Biol. (2005) [Pubmed]
  8. Targeted disruption of the mouse homologue of the Drosophila polyhomeotic gene leads to altered anteroposterior patterning and neural crest defects. Takihara, Y., Tomotsune, D., Shirai, M., Katoh-Fukui, Y., Nishii, K., Motaleb, M.A., Nomura, M., Tsuchiya, R., Fujita, Y., Shibata, Y., Higashinakagawa, T., Shimada, K. Development (1997) [Pubmed]
  9. Characterization of cis-elements required for the transcriptional activation of the rae28/mph1 gene in F9 cells. Motaleb, M.A., Takihara, Y., Ohta, H., Shimada, K. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  10. Sequence-specific DNA binding activity in the RAE28 protein, a mouse homologue of the Drosophila polyhomeotic protein. Nomura, M., Takihara, Y., Abdul Motaleb, M., Horie, K., Higashinakagawa, T., Shimada, K. Biochem. Mol. Biol. Int. (1998) [Pubmed]
  11. Structural organization of the rae28 gene, a putative murine homologue of the Drosophila polyhomeotic gene. Abdul Motaleb, M., Takihara, Y., Nomura, M., Matsuda, Y., Higashinakagawa, T., Shimada, K. J. Biochem. (1996) [Pubmed]
  12. Regulation of Hoxb3 expression in the hindbrain and pharyngeal arches by rae28, a member of the mammalian Polycomb group of genes. Tomotsune, D., Shirai, M., Takihara, Y., Shimada, K. Mech. Dev. (2000) [Pubmed]
  13. RAE28, BMI1, and M33 are members of heterogeneous multimeric mammalian Polycomb group complexes. Hashimoto, N., Brock, H.W., Nomura, M., Kyba, M., Hodgson, J., Fujita, Y., Takihara, Y., Shimada, K., Higashinakagawa, T. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
 
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