Chromodomain
| Chromodomain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of polycomb chromodomain.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Chromodomain | ||||||||
| Pfam | PF00385 | ||||||||
| InterPro | IPR000953 | ||||||||
| SMART | SM00298 | ||||||||
| PROSITE | PS50013 | ||||||||
| SCOP | 1pfb | ||||||||
| SUPERFAMILY | 1pfb | ||||||||
| 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]
See also
References
- ↑ Min J, Zhang Y, Xu RM (August 2003). "Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27". Genes Dev. 17 (15): 1823–8. doi:10.1101/gad.269603. PMC 196225. PMID 12897052.
- ↑ S Messmer, A Franke, R Paro (July 1992). "Analysis of the functional role of the Polycomb chromo domain in Drosophila melanogaster". Genes Dev. 6 (7): 1241–1254. doi:10.1101/gad.6.7.1241. PMID 1628830.
- ↑ Tajul-Arifin, K, Teasdale, R, Ravasi, T, Humel, DA, Group, RIKEN GER, Members, GSL, Mattick, JS. (2003). "Identification and Analysis of Chromodomain-Containing Proteins Encoded in the Mouse Transcriptome". Genome Res 13 (6B): 1416–1429. doi:10.1101/gr.1015703. PMC 403676. PMID 12819141.
- ↑ Jones, DO, Cowell, IG, Singh, PB. (2000). "Mammalian chromodomain proteins: their role in genome organisation and expression". Bioessays 22 (2): 124–37. doi:10.1002/(SICI)1521-1878(200002)22:2<124::AID-BIES4>3.0.CO;2-E. PMID 10655032.
- ↑ Nielsen, PR, Nietlispach, D, Mott, HR, Callaghan, J, Bannister, A, Kouzarides, T, Murzin, AG, Murzina, NV et al. (2002). "Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9". Nature 416 (6876): 103–7. doi:10.1038/nature722. PMID 11882902.
- ↑ Jacobs, SA, Khorasanizadeh, S. (2002). "Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail". Science 295 (5562): 2080–3. doi:10.1126/science.1069473. PMID 11859155.
- ↑ Verdel, A, Jia, S, Gerber, S, Sugiyama, T, Gygi, S, Grewal, S, Moazed, D (2004). "RNAi-Mediated Targeting of Heterochromatin by the RITS Complex". Science 303 (5658): 672–6. doi:10.1126/science.1093686. PMC 3244756. PMID 14704433.