| 词条 | Chromodomain |
| 释义 |
| Symbol = Chromodomain | Name = Chromodomain | image = PDB_1pfb_EBI.jpg | width = | caption = Structure of polycomb chromodomain.[1] | Pfam = PF00385 | InterPro = IPR000953 | SMART = SM00298 | PROSITE = PS50013 | SCOP = 1pfb | TCDB = | OPM family = | OPM protein = | 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
References1. ^{{cite journal |vauthors=Min J, Zhang Y, Xu RM |title=Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |journal=Genes Dev. |volume=17 |issue=15 |pages=1823–8 |date=August 2003 |pmid=12897052 |pmc=196225 |doi=10.1101/gad.269603 |url=}} 2. ^{{cite journal | vauthors = Messmer S, Franke A, Paro R | title = Analysis of the functional role of the Polycomb chromo domain in Drosophila melanogaster | journal = Genes Dev. | volume = 6 | issue = 7 | pages = 1241–1254 | date = July 1992 | pmid = 1628830 | doi = 10.1101/gad.6.7.1241 | url = }} 3. ^{{cite journal | vauthors = Tajul-Arifin K, Teasdale R, Ravasi T, Hume DA, Mattick JS | title = Identification and Analysis of Chromodomain-Containing Proteins Encoded in the Mouse Transcriptome | journal = Genome Res | volume = 13 | issue = 6B | pages = 1416–1429 | year = 2003 | pmid = 12819141 | pmc = 403676 | doi = 10.1101/gr.1015703 }} 4. ^{{cite journal | vauthors = Jones DO, Cowell IG, Singh PB | title = Mammalian chromodomain proteins: their role in genome organisation and expression | journal = BioEssays | volume = 22 | issue = 2 | pages = 124–37 | year = 2000 | pmid = 10655032 | doi = 10.1002/(SICI)1521-1878(200002)22:2<124::AID-BIES4>3.0.CO;2-E | citeseerx = 10.1.1.575.6410 }} 5. ^{{cite journal | vauthors = Nielsen PR, Nietlispach D, Mott HR, Callaghan J, Bannister A, Kouzarides T, Murzin AG, Murzina NV, Laue ED | title = Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9 | journal = Nature | volume = 416 | issue = 6876 | pages = 103–7 | year = 2002 | pmid = 11882902 | doi = 10.1038/nature722 }} 6. ^{{cite journal | vauthors = Jacobs SA, Khorasanizadeh S | title = Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail | journal = Science | volume = 295 | issue = 5562 | pages = 2080–3 | year = 2002 | pmid = 11859155 | doi = 10.1126/science.1069473 }} 7. ^{{cite journal | vauthors = Verdel A, Jia S, Gerber S, Sugiyama T, Gygi S, Grewal SI, Moazed D | title = RNAi-Mediated Targeting of Heterochromatin by the RITS Complex | journal = Science | volume = 303 | issue = 5658 | pages = 672–6 | year = 2004 | pmid = 14704433 | pmc = 3244756 | doi = 10.1126/science.1093686 }} External links
1 : Protein domains |
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