Chromodomain Explained

Symbol:	Chromodomain
Chromodomain
Pfam:	PF00385
Interpro:	IPR000953
Smart:	SM00298
Prosite:	PS50013
Scop:	1pfb
Cdd:	cd00024

A chromodomain (chromatin organization modifier^[1]) is a protein structural domain of about 40–50 amino acid residues commonly found in proteins associated with the remodeling and manipulation of chromatin. The domain is highly conserved among both plants and animals, and is represented in a large number of different proteins in many genomes, such as that of the mouse. Some chromodomain-containing genes have multiple alternative splicing isoforms that omit the chromodomain entirely.^[2] In mammals, chromodomain-containing proteins are responsible for aspects of gene regulation related to chromatin remodeling and formation of heterochromatin regions.^[3] Chromodomain-containing proteins also bind methylated histones^{[4] [5]} and appear in the RNA-induced transcriptional silencing complex.^[6] In histone modifications, chromodomains are very conserved. They function by identifying and binding to methylated lysine residues that exist on the surface of chromatin proteins and thereby regulate gene transcription.^[7]

See also

• Bromodomain
• Chromo shadow domain

External links

• Chromatin Remodeling: Chromodomains at cellsignal.com

Notes and References

1. Messmer S, Franke A, Paro R . Analysis of the functional role of the Polycomb chromo domain in Drosophila melanogaster . Genes Dev. . 6 . 7 . 1241–1254 . July 1992 . 1628830 . 10.1101/gad.6.7.1241 . free .
2. Tajul-Arifin K, Teasdale R, Ravasi T, Hume DA, Mattick JS . Identification and Analysis of Chromodomain-Containing Proteins Encoded in the Mouse Transcriptome . Genome Res . 13 . 6B . 1416–1429 . 2003 . 12819141 . 403676 . 10.1101/gr.1015703 .
3. Jones DO, Cowell IG, Singh PB . Mammalian chromodomain proteins: their role in genome organisation and expression . BioEssays . 22 . 2 . 124–37 . 2000 . 10655032 . 10.1002/(SICI)1521-1878(200002)22:2<124::AID-BIES4>3.0.CO;2-E . 10.1.1.575.6410 .
4. Nielsen PR, Nietlispach D, Mott HR, Callaghan J, Bannister A, Kouzarides T, Murzin AG, Murzina NV, Laue ED . Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9 . Nature . 416 . 6876 . 103–7 . 2002 . 11882902 . 10.1038/nature722 . 2002Natur.416..103N . 4423019 .
5. Jacobs SA, Khorasanizadeh S . Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail . Science . 295 . 5562 . 2080–3 . 2002 . 11859155 . 10.1126/science.1069473 . 2002Sci...295.2080J . 38589662 .
6. Verdel A, Jia S, Gerber S, Sugiyama T, Gygi S, Grewal SI, Moazed D . RNAi-Mediated Targeting of Heterochromatin by the RITS Complex . Science . 303 . 5658 . 672–6 . 2004 . 14704433 . 3244756 . 10.1126/science.1093686 . 2004Sci...303..672V .
7. Yap KL, Zhou MM . Structure and mechanisms of lysine methylation recognition by the chromodomain in gene transcription . Biochemistry . 50 . 12 . 1966–80 . March 2011 . 21288002 . 3062707 . 10.1021/bi101885m .