Please wait a minute...

中国生物工程杂志

China Biotechnology
China Biotechnology  2010, Vol. 30 Issue (06): 21-27    DOI: Q7;Q81
    
Localization of Histone Acetyltransferase PCAF in Nuclear Dot 10 Through Its Interaction with PML Protein
LI Ping-fa1,LIU Hui2,ZHAN He-qin3
1.Xinxiang Medical College, Xinxiang 453003, China
2.Central Hospital of Luoyangcity, Luoyang 471009, China
3.Department of Pharmaceutical College, Xinxiang Medical College, Xinxiang 453003, China
Download: HTML   PDF(798KB) HTML
Export: BibTeX | EndNote (RIS)      

Abstract  

As one of the important histone acetyltransferases, PCAF(P300/CBP associated factor) mainly mediates the acetylation of core histones and hence plays a vital role in the transcriptional regulation. Several cellular proteins that interact with PCAF directly, such as P300/CBP, p53 and MDM2, have been reported localized in nuclear dot 10 (ND10), an intranuclear structure with a typical discrete punctuate distribution. ND10 contains more than 70 kinds of proteins and has been implicated in the regulation of gene transcription. The most key component of ND10 is PML (promyelocytic leukemia protein). PML is well known to be essential for the maintenance of the normal structure and function of ND10. By the use of yeast two-hybridization, GST pull-down, co-immunoprecipitation and fluorescence colocalization assays,the evidence for the direct interaction of PCAF with PML and the localization of PCAF in ND10 was provided, which will be beneficial for the further research on the biological function of PCAF.



Key wordsP300/CBP associated factor      Promyelocytic leukemia protein      Nuclear dot 10     
Received: 23 December 2009      Published: 12 June 2010
Cite this article:

LI Beng-Fa, LIU Hui, DAN Ge-Qin. Localization of Histone Acetyltransferase PCAF in Nuclear Dot 10 Through Its Interaction with PML Protein. China Biotechnology, 2010, 30(06): 21-27.

URL:

https://manu60.magtech.com.cn/biotech/Q7;Q81     OR     https://manu60.magtech.com.cn/biotech/Y2010/V30/I06/21

[1] Schiltz R L, Mizzen C A, Vassilev A, et al. Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates. J Biol Chem, 1999, 274(3) :11891192. 
[2] Jensen K, Shiels C, Freemont P S. PML protein isoforms and the RBCC/TRIM motif. Oncogene, 2001, 20(49) :72237233. 
[3] Beech S J, Lethbridge K J, Killick N, et al. Isoforms of the promyelocytic leukemia protein differ in their effects on ND10 organization. Exp Cell Res, 2005, 307(1) :109117. 
[4] Everett R D, ChelbiAlix M K. PML and PML nuclear bodies: implications in antiviral defence. Biochimie, 2007, 89(67) :819830. 
[5] Negorev D, Maul G G. Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot. Oncogene, 2001, 20(49) :72347242. 
[6] Zhong S, Muller S, Ronchetti S, et al. Role of SUMO1modified PML in nuclear body formation. Blood, 2000, 95(9) :27482752. 
[7] Cho H, Orphanides G, Sun X, et al. A human RNA polymerase II complex containing factors that modify chromatin structure. Mol Cell Biol, 1998, 18(9) :53555363. 
[8] Liu L, Scolnick D M, Trievel R C, et al. p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage. Mol Cell Biol, 1999, 19(2) :12021209. 
[9] Jin Y, Zeng S X, Dai M S, et al. MDM2 inhibits PCAF (p300/CREBbinding proteinassociated factor)mediated p53 acetylation. J Biol Chem, 2002, 277(34) :3083830843. 
[10] Liu X, Tesfai J, Evrard Y A, et al. cMyc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation. J Biol Chem, 2003, 278(22) :2040520412. 
[11] Masumi A, Wang I M, Lefebvre B, et al. The histone acetylase PCAF is a phorbolesterinducible coactivator of the IRF family that confers enhanced interferon responsiveness. Mol Cell Biol, 1999, 19(3) :18101820. 
[12] Masumi A, Ozato K. Coactivator p300 acetylates the interferon regulatory factor2 in U937 cells following phorbol ester treatment. J Biol Chem, 2001, 276(24) :2097320980. 
[13] Kurooka H, Honjo T. Functional interaction between the mouse notch1 intracellular region and histone acetyltransferases PCAF and GCN5. J Biol Chem, 2000, 275(22) :1721117220. 
[14] Yao Y L, Yang W M, Seto E. Regulation of transcription factor YY1 by acetylation and deacetylation. Mol Cell Biol, 2001, 21(17) :59795991. 
[15] Doucas V, Tini M, Egan D A, et al. Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling. Proc Natl Acad Sci U S A, 1999, 96(6) :26272632. 
[16] Guo A, Salomoni P, Luo J, et al. The function of PML in p53dependent apoptosis. Nat Cell Biol, 2000, 2(10) :730736. 
[17] Wei X, Yu Z K, Ramalingam A, et al. Physical and functional interactions between PML and MDM2. J Biol Chem, 2003, 278(31) :2928829297. 
[18] Zhong S, Salomoni P, Pandolfi P P. The transcriptional role of PML and the nuclear body. Nat Cell Biol, 2000, 2(5) :8590. 
[19] Boisvert F M, Kruhlak M J, Box A K, et al. The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body. J Cell Biol, 2001, 152(5) :10991106. 
[20] Hayakawa F, Abe A, Kitabayashi I, et al. Acetylation of PML is involved in histone deacetylase inhibitormediated apoptosis. J Biol Chem, 2008, 283(36) :2442024425.

No related articles found!