Biology:Chromodomain
| Chromodomain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of polycomb chromodomain.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Chromodomain | ||||||||
| Pfam | PF00385 | ||||||||
| InterPro | IPR000953 | ||||||||
| SMART | SM00298 | ||||||||
| PROSITE | PS50013 | ||||||||
| SCOP2 | 1pfb / SCOPe / SUPFAM | ||||||||
| CDD | cd00024 | ||||||||
| |||||||||
A chromodomain (chromatin organization modifier[2]) 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.[3] In mammals, chromodomain-containing proteins are responsible for aspects of gene regulation related to chromatin remodeling and formation of heterochromatin regions.[4] Chromodomain-containing proteins also bind methylated histones[5][6] and appear in the RNA-induced transcriptional silencing complex.[7] 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.[8]
See also
References
- ↑ "Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27". Genes Dev. 17 (15): 1823–8. August 2003. doi:10.1101/gad.269603. PMID 12897052.
- ↑ "Analysis of the functional role of the Polycomb chromo domain in Drosophila melanogaster". Genes Dev. 6 (7): 1241–1254. July 1992. doi:10.1101/gad.6.7.1241. PMID 1628830.
- ↑ "Identification and Analysis of Chromodomain-Containing Proteins Encoded in the Mouse Transcriptome". Genome Res 13 (6B): 1416–1429. 2003. doi:10.1101/gr.1015703. PMID 12819141.
- ↑ "Mammalian chromodomain proteins: their role in genome organisation and expression". BioEssays 22 (2): 124–37. 2000. doi:10.1002/(SICI)1521-1878(200002)22:2<124::AID-BIES4>3.0.CO;2-E. PMID 10655032.
- ↑ "Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9". Nature 416 (6876): 103–7. 2002. doi:10.1038/nature722. PMID 11882902.
- ↑ "Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail". Science 295 (5562): 2080–3. 2002. doi:10.1126/science.1069473. PMID 11859155.
- ↑ "RNAi-Mediated Targeting of Heterochromatin by the RITS Complex". Science 303 (5658): 672–6. 2004. doi:10.1126/science.1093686. PMID 14704433.
- ↑ "Structure and mechanisms of lysine methylation recognition by the chromodomain in gene transcription". Biochemistry 50 (12): 1966–80. March 2011. doi:10.1021/bi101885m. PMID 21288002.
External links
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