染色质重构因子CHD蛋白家族的研究进展

王会平; 徐勤枝; 周平坤

染色质重构因子CHD蛋白家族的研究进展

王会平 , 徐勤枝 , 周平坤

文章导航 > 国际放射医学核医学杂志 > 2006, 30 > 1: (42-47)

引用本文:

Citation:

染色质重构因子CHD蛋白家族的研究进展

100850 北京, 军事医学科学院放射医学研究所放射毒理与辐射危害评价研究室
基金项目:
国家自然科学基金资助项目(30270423)
中图分类号: Q753

Progress on chromatin remodeling factor CHD

Department of Radiation Toxicology and Detriment Assessment, Beijing Institute of Radiation Medicine, Beijing 100850, China
CLC number: Q753

摘要: 染色质重构是DNA修复、基因表达调控过程中的一个重要环节。染色质重构使染色质组织结构发生一系列重要的变化,如染色质去凝集,核小体变成开放式的疏松结构,使转录因子等更易接近并结合核小体DNA,从而调控基因转录等。CHD蛋白是目前已知的染色质重构复合物之一。目前已鉴定了6个人类CHD蛋白成员,主要有3种功能结构域:N端的两个染色质调节域,位于中部的类SWI2/SNF2 ATP酶/解旋酶域,以及C端的DNA结合域。CHD基因突变或表达异常与人类某些疾病有关。
- 染色质重构 /
- ATP酶 /
- CHD /
- SWI2/SNF2
Abstract: Chromatin remodeling plays an important role in DNA repair, gene transcriptional regulation. Remodeling resultes in a series of important changes in chromatin structure, e.g. loosing the condensed chromatin and opening the structure of nucleosome, which leads to increased accessibility of the transcription factors to nucleosomal DNA. CHD (chromodomain, helicase, DNA-binding) genes compose a subfamily of the known chromatin remodeling complexes. Up to now, six human CHD members have been cloned. They contain three main domains:Chromodomain which locates in the N terminus of the proteins, SWI2/SNF2-related ATPase/helicase domain in the middle region, DNA-binding domain in the C terminus. The mutation or abnor-mal expression of CHD gene is thought to be related to some human diseases.
- Chromatin remodeling /
- ATPase /
- CHD /
- SW12/SNF2
本作品遵循Signature-Non-Commercial Use 4.0 International (CC BY-NC 4.0)协议

[1]	Tran HG,Steger DJ,Iyer VR,et al.The chromo domain protein chd 1p fom budding yeast is an ATP-dependent chromatinmodifying factor.EMBO J,2000,19(10):2323-2331.
[2]	Tai HH,Geisterfer M,Bell JC,et al.CHD1 associates with NCoR and histone deacetylase as well as with RNA splicing proteins.Biochem Biophy Res Com,2003,308:170-176.
[3]	Hosoi Y,Miyachi H,Matsumoto Y,et al.Induction of interleukin-1beta and interleukin-6 Mrna by low doses of ionizing radiation in macrophages.Int J Cancer,2001,96(5):270-276.
[4]	Robson T,Joiner MC,McCullough W,et al.A novel human stressrelated gene with a potential role in induced resisance.Radiat Res,1999,152(5):451-461.
[5]	Kelley DE,Stokes DG,Perry RP.CHD1 interacts with SSRP1 and depends on both its chromodomain and its ATPase/helicase-like domain for proper association with chromatin.Chromosoma,1999,108(1):10-25.
[6]	Dellaire G,Makarov EM,Cowger JJ,et al.Mammalian PRP4 kinase copurifies and interacts with components of both the U5 snRNP and the N-CoR deacetylase complexes.Mol Cell Biol,2002,22(14):5141-5156.
[7]	Thompson PM,Gotoh T,Kok M,et al.CHD5,a new member of the chromodomain gene family,is preferentially expressed in the nervous system.Oncogene,2003,22(7):1002-1011.
[8]	Bench AJ,Nacheva EP,Hood TL,et al.Chromosome 20 deletions in myeloid malignancies:reduction of the common deleted region,generation of a PAC/BAC contig and identification of candidate genes.Oncogene,2000,19(34):3902-3913.
[9]	孙志增, 徐勤枝, 隋建丽, 等.辐射诱导转录子RIGb cDNA对Hela细胞增殖的抑制作用.中国生物化学与分子生物学报,2005,21(3):384-389.
[10]	辐射诱导基因LRIGx的细胞周期特异性表达及编码产物同源性分析.中国生物化学与分子生物学报,2002(3 ).
[11]	Linder B,Gerlach N,Jackle H.The drosophila homolog of the human AF10 is an HP1-interacting suppressor of position effect variegation.EMBO Rep,2004,5(10):1013.
[12]	Belyaeva ES,Boldyreva LV,Volkova EI,et al.Effect of the suppressor of underreplication (SuUR) gene on position-effect variegation silencing in drosophila melanogaster.Genetics,2003,165(3):1209-1220.
[13]	Kehle J,Beuchle D,Treuheit S,et al.dMi-2,a hunchback-interacting protein that functions in polycomb repression.Science,1998,282(5395):1897-1900.
[14]	Woodage T,Basrai MA,Baxevanis AD,et al.Characterization of the CHD family of proteins.Proc Natl Acad Sci USA,1997,94(21):11472-11477.
[15]	Kwon HA,Imbalzano N,Khavari PA,et al.Nucleosome disruption and enhancement of activator binding by a human SWI/SNF complex.Nature,1994,370:477-481.
[16]	Tong JK,Hassig CA,Schnitzler GR,et al.Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex.Nature,1998,395(6705):917-921.
[17]	Bowen NJ,Fujita N,Kajita M,et al.Mi-2/NuRD:multiple complexes for many purposes.Biochim Biophys Acta,2004,15(1-3):52-57.
[18]	Wade PA,Gegonne A,Jones PL,et al.Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation.Nat Genet,1999,23(1):62-66.
[19]	Zhang Y,Ng HH,Erdjument-Bromage H,et al.Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation.Genes Dev,1999,13(15):1924-1935.
[20]	Guschin D,Wade PA,Kikyo N,et al.ATP-Dependent histone octamer mobilization and histone deacetylation mediated bythe Mi-2chromatin remodeling complex.Biochemistry,2000,39(18):5238-5245.
[21]	Dean Rider SJr,Henderson JT,Jerome RE,et al.Coordinate repression of regulators of embryonic identity by PICKLE during germination in Arabidopsis.Plant J,2003,35(1):33-43.
[22]	Shimono Y,Murakami H,Kawai K,et al.Mi-2 beta associates with BRG1 and RET finger protein at the distinct regions with transcriptional activating and repressing abilities.J Biol Chem,2003,278(51):51638-51645.
[23]	Khorasanizadeh S.The nucleosome:from genomic organization to genomic regulation.Cell,2004,116(2):259-272.
[24]	Fyodorov DV,Kadonaga JT.The many faces of chromatin remodeling:SWItching beyond transcription.Cell,2001,106(5):523-525.
[25]	Xue Y,Canman JC,Lee CS,et al.The human SWI/SNF-B chromatinremodeling complex is related to yeast RSC and localizes at kinetochores of mitotic chromosomes.Proc Natl Acad Sci USA,2000,97(24):13015-13020.
[26]	Seelig HP,Moosbrugger I,Ehrfeld H,et al.The major dermatomyositis-specific Mi-2 autoantigen is a presumed helicase involved in transcriptional activation.Arthritis Rheum,1995,38(10):1389-1399.
[27]	Nilasena DS,Trieu EP,Targoff IN.Analysis of the Mi-2 autoantigen of dermatomyositis.Arthritis Rheum,1995,38(1):123-128.
[28]	Xue Y,Wong J,Moreno GT,et al.NURD,a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities.Mol Cell,1998,2(6):851-861.
[29]	Horn PJ,Carruthers LM,Logie C,et al.Phosphorylation of linker histones regulates ATP-dependent chromatin remodeling enzymes.Nat Struct Biol,2002,9(4):263-267.

[1]	李桂荣 , 陆如山 . 碱性核酸内切酶在正常和照射小鼠的胸腺、脾及肝细胞核释放可溶性染色质中的作用. 国际放射医学核医学杂志, 1980, 4(3): 195-195.
[2]	王兆霖 , 罗祖玉 . 染色质结构是哺乳动物细胞中辐射诱导的DNA单链断裂和重接的一个因素. 国际放射医学核医学杂志, 1984, 8(2): 102-103.
[3]	段红 , 牛惠生 . 染色质结构对辐射所致DNA链断裂频率的影响:用核及拟核单层技术的研究. 国际放射医学核医学杂志, 1992, 16(5): 215-216.
[4]	周乐源 , 周菊英 . 环氧合酶-2抑制剂及其辐射增敏效应. 国际放射医学核医学杂志, 2005, 29(3): 129-131.
[5]	李晴 , 王璐 , 徐畅 , 王彦 , 杜利清 , 王芹 , 杨福军 , 孙元明 , 刘强 . 姜油树脂对辐射后间充质干细胞Nrf2及其靶基因表达的影响. 国际放射医学核医学杂志, 2015, 39(5): 389-392. doi: 10.3760/cma.j.issn.1673-4114.2015.05.008
[6]	李章 , 周元恺 . 吸入²³⁸PuO₂-ZrO₂粒子引起叙利亚腮鼠肺细胞的染色体畸变. 国际放射医学核医学杂志, 1979, 3(1): 64-64.
[7]	李桂荣 , 宋小英 . WR-2721对照射诱发红细胞和微粒体内脂质过氧化和酶释放的影响. 国际放射医学核医学杂志, 1990, 14(5): 210-211.
[8]	莫启忠 , 宫斌 , 彭再鸣 . ¹²⁵I-标记的依赖Ca⁺²调节蛋白与环核苷酸磷酸二酯酶和其抑制蛋白的相互作用. 国际放射医学核医学杂志, 1980, 4(2): 133-133.
[9]	陈德政 , 葛忠良 , 郭裕中 . ATP对腹部局部受照小鼠小肠机能的影响. 国际放射医学核医学杂志, 1982, 6(1): 54-56.
[10]	何庆加 , 孙世镇 , 穆传杰 . 照射G₁或G₂期细胞后第二次细胞分裂时染色体畸变类型. 国际放射医学核医学杂志, 1994, 18(4): 165-165.

点击查看大图

计量

文章访问数: 1060
HTML全文浏览量: 76
PDF下载量: 2

染色质重构因子CHD蛋白家族的研究进展

100850 北京, 军事医学科学院放射医学研究所放射毒理与辐射危害评价研究室

收稿日期: 2005-04-01

基金项目: 国家自然科学基金资助项目(30270423)

关键词:

染色质重构 /
ATP酶 /
CHD /
SWI2/SNF2

摘要: 染色质重构是DNA修复、基因表达调控过程中的一个重要环节。染色质重构使染色质组织结构发生一系列重要的变化,如染色质去凝集,核小体变成开放式的疏松结构,使转录因子等更易接近并结合核小体DNA,从而调控基因转录等。CHD蛋白是目前已知的染色质重构复合物之一。目前已鉴定了6个人类CHD蛋白成员,主要有3种功能结构域:N端的两个染色质调节域,位于中部的类SWI2/SNF2 ATP酶/解旋酶域,以及C端的DNA结合域。CHD基因突变或表达异常与人类某些疾病有关。