Difference between revisions of "Part:BBa J176000"

Revision as of 04:54, 3 July 2011

hPCD

Polycomb chromodomain (PCD) from the human CBX8 protein (a.a. 1-63).

Usage and Biology

The Polycomb crhomodomain (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:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 1: / Line 1: @@
 __NOTOC__
 <partinfo>BBa_J176000 short</partinfo>
-Human Polycomb chromodomain from the CBX8 protein (a.a. 1-63).
+Polycomb chromodomain (PCD) from the human CBX8 protein (a.a. 1-63).
-See Haynes and Silver, JBC, 2011
-<!-- Add more about the biology of this part here
 ===Usage and Biology===
+The Polycomb crhomodomain (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.
 <!-- -->