Difference between revisions of "Part:BBa J176000"
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===Usage and Biology=== | ===Usage and Biology=== | ||
| − | [[Image:Haynes_CBX8_PDB3I91.png|thumb|250px|'''Human PCD of CBX8''' (orange) Crystal structure reported by Kaustov et al. 2011. Grey = H3 histone tail; Ball and stick = trimethylated lysine | + | [[Image:Haynes_CBX8_PDB3I91.png|thumb|250px|'''Human PCD of CBX8''' (orange) Crystal structure reported by Kaustov et al. 2011. Grey = H3 histone tail; Ball and stick = trimethylated lysine 9 ]] |
* Protein Data Bank ID 3I91 | * Protein Data Bank ID 3I91 | ||
| − | * Mammalian expression vector | + | * Mammalian expression vector recommended |
| − | * Protein domain; | + | * Protein domain; has start codon; requires promoter, stop codon, and polyA signal for proper expression<br> |
The Polycomb chromodomain (PCD) is an ancient protein motif that is conserved in many multicellular organisms (from plants to insects to humans). The motif appears in proteins involved in regulating tissue identity, including the Drosophila (fruit fly) Pc protein, and the vertebrate Chromobox (CBX) protein family. PCD has an aromatic pocket that specifically recognizes the unfolded "tail" of histone H3 when the histone is trimethylated at lysine 27. Early characterization of this domain was done by Fischle et al (2003) and Min et al. (2003). The 3D structures for several human homologues have been reported (Kaustov et al., 2011). | The Polycomb chromodomain (PCD) is an ancient protein motif that is conserved in many multicellular organisms (from plants to insects to humans). The motif appears in proteins involved in regulating tissue identity, including the Drosophila (fruit fly) Pc protein, and the vertebrate Chromobox (CBX) protein family. PCD has an aromatic pocket that specifically recognizes the unfolded "tail" of histone H3 when the histone is trimethylated at lysine 27. Early characterization of this domain was done by Fischle et al (2003) and Min et al. (2003). The 3D structures for several human homologues have been reported (Kaustov et al., 2011). | ||
| − | <br>In its native context, the PCD targets gene silencing proteins to genes marked with histone methylation. The PCD domain can be fused to Biobrick proteins to recruit other protein domains, such as synthetic transcriptional activators, to sites of histone methylation in human cells (Haynes and Silver, 2011). | + | <br>In its native context, the PCD targets gene silencing proteins to genes marked with histone methylation. The PCD domain can be fused to Biobrick proteins to recruit other protein domains, such as synthetic transcriptional activators, to sites of histone methylation in human cells (Haynes and Silver, 2011). Note that the solved 3D structure shows the human CBX8 PCD bound to methylated histone H3 lysine 9, but biochemical tests have shown that it prefers methylated lysine 27. |
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Latest revision as of 19:16, 6 April 2012
hPCD
Polycomb chromodomain (PCD) from the human CBX8 protein (a.a. 1-63).
Alias: KAH01
Usage and Biology
- Protein Data Bank ID 3I91
- Mammalian expression vector recommended
- Protein domain; has start codon; requires promoter, stop codon, and polyA signal for proper expression
The Polycomb chromodomain (PCD) is an ancient protein motif that is conserved in many multicellular organisms (from plants to insects to humans). The motif appears in proteins involved in regulating tissue identity, including the Drosophila (fruit fly) Pc protein, and the vertebrate Chromobox (CBX) protein family. PCD has an aromatic pocket that specifically recognizes the unfolded "tail" of histone H3 when the histone is trimethylated at lysine 27. Early characterization of this domain was done by Fischle et al (2003) and Min et al. (2003). The 3D structures for several human homologues have been reported (Kaustov et al., 2011).
In its native context, the PCD targets gene silencing proteins to genes marked with histone methylation. The PCD domain can be fused to Biobrick proteins to recruit other protein domains, such as synthetic transcriptional activators, to sites of histone methylation in human cells (Haynes and Silver, 2011). Note that the solved 3D structure shows the human CBX8 PCD bound to methylated histone H3 lysine 9, but biochemical tests have shown that it prefers methylated lysine 27.
REFERENCES:
- Fischle, W, Wang, Y, Jacobs, SA, Kim, Y, Allis, CD, Khorasanizadeh, S. (2003) Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains. Genes Dev. 17:1870-1881.
- Min, J, Zhang, Y, Xu, RM. (2003) Structural basis for the specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. Genes Dev. 17:1823-1828.
- Haynes, KA, Silver, PA. (2011) Synthetic reversal of epigenetic silencing. J Biol Chem. 286:27176-27182.
- Kaustov, L., Ouyang, H., Amaya, M., Lemak, A., Nady, N., Duan, S., Wasney, G.A., Li, Z., Vedadi, M., Schapira, M., Min, J., Arrowsmith, C.H. (2011) Recognition and specificity determinants of the human cbx chromodomains. J Biol Chem. 286:521-529.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]