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腺病毒E1B55ku癌蛋白打破hDaxx与PML在细胞核的共定位 被引量：8

DISRUPTION OF CO-LOCATION OF hDaxx WITH PML IN NUCLEI BY ADENOVIRUS E1B 55 ku ONCOPROTEINS
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摘要 利用间接免疫荧光试验 ,通过Confocal激光扫描生物荧光显微镜和图像软件分析腺病毒 (adenovirus,Ad)E1B 5 5ku癌蛋白 (AdE1B 5 5ku)与人Daxx(humanDaxx ,hDaxx)在细胞核的定位关系 ,研究它对早幼粒细胞性白血病蛋白 (promyelocyticleukemiaprotein ,PML)与hDaxx在细胞核定位关系的影响。实验结果表明 ,AdE1B 5 5ku与hDaxx共定位细胞核 ,并打破hDaxx与PML共定位于细胞核PML致癌结构域 (PMLoncogenicdomains,PODs) Co location relation of oncoproteins (Ad E1b 55 ku) of adenovirus (Ad) E1b 55 ku with human Daxx (hDaxx) in nuclei was analyzed using indirect immuno fluorescent testing, Confocal laser scanning bio fluorescent microscope, and image software. Its effect to the location relation in nuclei to promyelocytic leukemia protein was studied. The results showed that Ad E1B 55 ku (or Ad12 55 ku) co localized with hDaxx in nuclei of G401 CC3 cells. And Ad5 E1B 55 ku or Ad12 E1B 55 ku disrupted the co location of hDaxx with PML in PODs (PML oncogenic domains) in nuclei of G401 CC3 or 293 cells.
作者 万艳平 谭立志 刘传爱 吴移谋 Colosimo April 廖代清
机构地区 南华大学基础医学院病原生物学研究所 加拿大Sherbrooke大学医学院微生物学与感染学系 美国Florida大学医学院解剖学与细胞生物学系
出处 《微生物学杂志》 CAS CSCD 2001年第4期46-48,共3页 Journal of Microbiology
基金 加拿大Sherbrooke大学医学院微生物学与感染学系廖代清博士实验室资助
关键词 腺病毒E1B55ku癌蛋白 HDAXX PML 细胞核 共定位 感染 Adenovirus E1B 55 ku, oncoprotein, hDaxx, PML.
分类号 R373.9 [医药卫生—病原生物学]
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参考文献5

  • 1[1]Wienzek, S., Roth, J. and Dobbelstein, M. E1B 55-kilodalton oncoproteins of adenovirus types 5 and 12 inactivate and relocalize p53, but not p51 or p73, and cooperate with EAorf6 proteins to destabilize p53[J]. J. Virol., 2000,74:193～202.
  • 2[2]Punga, T. and Akusjarvi, G. The adenovirus-2 E1B-55K protein interacts with a mSin3A/histone deacetylase 1 complex[J]. FEBS Letters, 2000,476:248～252.
  • 3[3]Liu, y., Colosimo, A.L., Yang, X.J., etal. Adenovirus E1B 55-kilodalton oncoprotein inhibits p53 acetylation by PCAF[J].Mol. & Cell. Biol., 2000,20:5540～5553.
  • 4[4]Ishov, M., A., Sotnikov, G., A., Negorev, D., et al. PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1[J].J. Cell Biology, 1999,147: 221 ～ 233.
  • 5[5]Li, H., Leo, C., Zhu, J., et al. Sequestration and inhibition of Daxx-mediated transcriptional repression by PML[J]. Molecular and cellular biology, 2000,20:1784 ～ 1796.

同被引文献32

  • 1Yang X, Khosravi FR, Chang HY, et al. Daxx, a novel Fas-binding protein that activates JNK and apoptosis[J]. Cell, 1997, 89(7): 1067-1076.
  • 2Pluta AF, Earnshaw WC, Goldberg IG. Interphase-specific association of intrinsic centromere protein CENP-C with hDaxx, a death domain-binding protein implicated in Fas-mediated cell death[J]. Cell Sci, 1998, 111(14) : 2029-2041.
  • 3Ko YG, Kang YS, Park H, et al. Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm[J]. J Biol Chem, 2001, 276(42): 39103-39106.
  • 4Charette SJ, Lavoie JN, Lambert H, et al. Inhibition of Daxx-mediated apoptosis by heat shock protein 27[J]. Mol Cell Biol, 2000, 20(20): 7602-7612.
  • 5Muromoto R, Yamamoto T, Yumioka T, et al. Daxx enhances Fas-mediated apoptosis in a murine pro-B cell line, BAF3[J]. FEBS Lett, 2003, 540(1-3): 223-228.
  • 6Shinoda S, Skradski SL, Araki T, et al. Formation of a tumour necrosis factor receptor 1 molecular scaffolding complex and activation of apoptosis signal-regulating kinase 1 during seizure-induced neuronal death[J] . Eur J Neurosci, 2003, 17(10): 2065-2076.
  • 7Zhong S, Salomoni P, Ronchetti S, et al. Promyelocytic Leukemia Protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis[J]. J Exp Med, 2000, 191(4): 631-640.
  • 8Michaelson JS, Bader D, Kuo F, et al. Loss of Daxx, a promiscuously interacting protein, results in extensive apoptosis in early mouse development[J]. Genes Dev, 1999, 13(15): 1918-1923.
  • 9Liu Y, Colosimo AL, Yang XJ, et al. Adenovirus E1B 55-kilodalton oncoprotein inhibits p53 acetylation by PCAF[J]. Mol Cell Biol, 2000, 20(15): 5540-5553.
  • 10Zhao LY, Colosimo AL, Liu Y, et al. Adenovirus E1B 55-kilodalton oncoprotein binds to Daxx and eliminates enhancement of p53-dependent transcription by Daxx[J]. Virology, 2003, 77(21): 11809-11821.

引证文献8

二级引证文献9

微生物学杂志
2001年 第4期

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