Difference between revisions of "Part:BBa J176000"
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The Polycomb chromodomain (PCD) is a protein sequence motif that is conserved in many metazoans. PCD has an aromatic pocket that specifically recognizes the unfolded "tail" of histone H3 when the histone is trimethylated at lysine 27. The crystal structure has been solved for the Drosophila melanogaster (fruit fly) variant this peptide (see figure below) (Fischle et al., 2003; see also Min et al., 2003). | The Polycomb chromodomain (PCD) is a protein sequence motif that is conserved in many metazoans. PCD has an aromatic pocket that specifically recognizes the unfolded "tail" of histone H3 when the histone is trimethylated at lysine 27. The crystal structure has been solved for the Drosophila melanogaster (fruit fly) variant this peptide (see figure below) (Fischle et al., 2003; see also Min et al., 2003). | ||
| − | [[Image:PCD_Fischle_2003|300px]] | + | [[Image:PCD_Fischle_2003.tif|300px]] |
This domain can be fused to other Biobrick proteins to recruit the fusion protein to sites of histone methylation in human cells (Haynes and Silver, 2011). | This domain can be fused to other Biobrick proteins to recruit the fusion protein to sites of histone methylation in human cells (Haynes and Silver, 2011). | ||
Revision as of 05:02, 3 July 2011
hPCD
Polycomb chromodomain (PCD) from the human CBX8 protein (a.a. 1-63).
Usage and Biology
The Polycomb chromodomain (PCD) is a protein sequence motif that is conserved in many metazoans. PCD has an aromatic pocket that specifically recognizes the unfolded "tail" of histone H3 when the histone is trimethylated at lysine 27. The crystal structure has been solved for the Drosophila melanogaster (fruit fly) variant this peptide (see figure below) (Fischle et al., 2003; see also Min et al., 2003).
This domain can be fused to other Biobrick proteins to recruit the fusion protein to sites of histone methylation in human cells (Haynes and Silver, 2011).
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. E-pub ahead of print.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]