Abstract
DNA is packed together with histone proteins in cell nuclei to form a compact structure called chromatin. Chromatin represents a scaffold for many genetic events and shows varying degrees of condensation, including a relatively open form (euchromatin) and a highly condensed form (heterochromatin). Enzymes such as histone acetyltransferases (HATs) and methylases covalently label the amino‐termini of histones, thereby creating a ‘histone code’ of modifications that is interpreted by the recruitment of other proteins through recognition domains. Ultimately, this network of interacting proteins is thought to control the degree of chromatin condensation so that DNA is available when it is required for genomic processes. Reviewed here are the structures of HAT and SET domains, which mediate the acetylation and methylation of histones, respectively, and bromodomains and chromodomains, which recognize the modified histones. How these structures have increased our understanding of DNA regulation is also discussed.
References
49
Referenced
79
10.1038/35030169
10.1073/pnas.51.5.786
10.1093/embo-reports/kvf013
10.1038/89675
10.1093/emboj/21.10.2430
10.1093/emboj/20.1.165
10.1016/S0092-8674(00)00118-5
10.1016/S1097-2765(03)00288-0
10.1128/MCB.22.3.874-885.2002
10.1038/20974
10.1093/embo-reports/kvf053
10.1038/nature01411
10.1038/nature02017
10.1016/S0955-0674(03)00013-9
10.1101/gad.1110503
10.1016/S0092-8674(03)00480-X
10.1016/S1097-2765(03)00273-9
10.1016/S1097-2765(02)00826-2
10.1126/science.1069473
10.1093/embo-reports/kve022
10.1002/(SICI)1521-1878(200002)22:2<124::AID-BIES4>3.0.CO;2-E
10.1016/S1097-2765(03)00482-9
10.1038/sj.embor.embor941
10.1038/38444
10.1038/35073047
10.1006/jmbi.2001.4859
10.1016/S0968-0004(03)00004-5
10.1101/gad.269603
10.1016/S1097-2765(02)00483-5
10.1016/S1097-2765(03)00528-8
10.1038/nature722
10.1093/emboj/19.22.6141
{'key': 'e_1_2_7_34_1', 'first-page': '217', 'article-title': 'The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA‐binding folds', 'volume': '9', 'author': 'Qiu C', 'year': '2002', 'journal-title': 'Nat Struct Biol'}
/ Nat Struct Biol / The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA‐binding folds by Qiu C (2002)10.1016/j.jmb.2004.01.051
10.1038/nature01080
10.1073/pnas.1735528100
10.1093/emboj/cdg273
10.1016/S0022-2836(03)00148-7
10.1128/MMBR.64.2.435-459.2000
10.1038/47412
10.1073/pnas.96.26.14967
10.1084/jem.20031291
10.1016/S0092-8674(01)00527-X
10.1016/S1097-2765(02)00802-X
10.1038/nature01378
10.1093/emboj/cdg326
10.1128/MCB.21.1.156-163.2001
10.1016/S1097-2765(03)00224-7
10.1101/gad.1156403
Dates
Type | When |
---|---|
Created | 21 years, 1 month ago (July 30, 2004, 1:24 a.m.) |
Deposited | 1 year, 8 months ago (Dec. 18, 2023, 3:57 p.m.) |
Indexed | 3 months ago (May 28, 2025, 5:46 p.m.) |
Issued | 21 years, 4 months ago (May 1, 2004) |
Published | 21 years, 4 months ago (May 1, 2004) |
Published Online | 21 years, 4 months ago (May 1, 2004) |
Published Print | 21 years, 4 months ago (May 1, 2004) |
@article{Bottomley_2004, title={Structures of protein domains that create or recognize histone modifications}, volume={5}, ISSN={1469-3178}, url={http://dx.doi.org/10.1038/sj.embor.7400146}, DOI={10.1038/sj.embor.7400146}, number={5}, journal={EMBO reports}, publisher={Springer Science and Business Media LLC}, author={Bottomley, Matthew J}, year={2004}, month=may, pages={464–469} }