|
Originally published In Press as doi:10.1074/jbc.M504904200 on August 23, 2005
J. Biol. Chem., Vol. 280, Issue 43, 36283-36292, October 28, 2005
Hsp90 Recruited by Sp1 Is Important for Transcription of 12(S)-Lipoxygenase in A431 Cells*
Jan-Jong Hung ,
Chih-Ying Wu ,
Pao-Chi Liao , and
Wen-Chang Chang 1
From the
Departments of Pharmacology and Occupational Health, College of Medicine, National Cheng Kung University, Tainan 701, Taiwan
Sp1 is a basic transcriptional factor that binds to the GC-rich region in the promoter of the target gene. It is involved in transcription of numerous genes by recruiting transcriptional factors to the promoters of target genes. In this study, we found in vivo and in vitro that Hsp90 was recruited to the GC-rich region of the 12(S)-lipoxygenase promoter through interaction with Sp1 in A431 cells by employing DNA affinity immunoprecipitation assay and chromatin immunoprecipitation assay. When Hsp90 was inhibited by geldanamycin (GA, a specific inhibitor of the Hsp90 family) or by siRNA of Hsp90 (to block its activity or to knockdown protein levels), respectively, luciferase activity (driven by the 12(S)-lipoxygenase promoter) and both mRNA and protein levels of 12(S)-lipoxygenase were reduced significantly in cells. In addition, the effect of GA was abolished when the Sp1 binding sites of 12(S)-lipoxygenase were mutated in A431 cells. Interestingly, binding of Sp1 to the 12(S)-lipoxygenase promoter was also decreased upon GA treatment in cells. In conclusion, our results indicate that Sp1 interacts with Hsp90 to recruit it to the promoter of 12(S)-lipoxygenase and then to regulate gene transcription by modulating the binding ability of Sp1 to promoters.
Received for publication, May 4, 2005
, and in revised form, August 11, 2005.
* This work was supported by the Ministry of Education Program for Promoting Academic Excellence of the University under Grant 91-B-FA09-1-4 and Grant NSC 94-2320-B-006-094 from the National Science Council of Taiwan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
1 To whom correspondence should be addressed: Dept. of Pharmacology, College of Medicine, National Cheng Kung University, Tainan 701, Taiwan. Tel.: 886-6-2353535 (ext. 5496); Fax: 886-6-2749296; E-mail: wcchang{at}mail.ncku.edu.tw.

CiteULike Complore Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
M. Tariq, U. Nussbaumer, Y. Chen, C. Beisel, and R. Paro
Trithorax requires Hsp90 for maintenance of active chromatin at sites of gene expression
PNAS,
January 27, 2009;
106(4):
1157 - 1162.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
R. H. Kim, R. Kim, W. Chen, S. Hu, K.-H. Shin, N.-H. Park, and M. K. Kang
Association of hsp90 to the hTERT promoter is necessary for hTERT expression in human oral cancer cells
Carcinogenesis,
December 1, 2008;
29(12):
2425 - 2431.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
S. H. Fisher and L. V. Wray Jr.
Bacillus subtilis glutamine synthetase regulates its own synthesis by acting as a chaperone to stabilize GlnR-DNA complexes
PNAS,
January 22, 2008;
105(3):
1014 - 1019.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
K. Camphausen and P. J. Tofilon
Inhibition of Hsp90: A Multitarget Approach to Radiosensitization
Clin. Cancer Res.,
August 1, 2007;
13(15):
4326 - 4330.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
C. Albanesi, H. R. Fairchild, S. Madonna, C. Scarponi, O. De Pita, D. Y. M. Leung, and M. D. Howell
IL-4 and IL-13 Negatively Regulate TNF-{alpha}- and IFN-{gamma}-Induced beta-Defensin Expression through STAT-6, Suppressor of Cytokine Signaling (SOCS)-1, and SOCS-3
J. Immunol.,
July 15, 2007;
179(2):
984 - 992.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
Y. Chen, M. P. Schnetz, C. E. Irarrazabal, R.-F. Shen, C. K. Williams, M. B. Burg, and J. D. Ferraris
Proteomic identification of proteins associated with the osmoregulatory transcription factor TonEBP/OREBP: functional effects of Hsp90 and PARP-1
Am J Physiol Renal Physiol,
March 1, 2007;
292(3):
F981 - F992.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
H. Dote, W. E. Burgan, K. Camphausen, and P. J. Tofilon
Inhibition of hsp90 compromises the DNA damage response to radiation.
Cancer Res.,
September 15, 2006;
66(18):
9211 - 9220.
[Abstract]
[Full Text]
[PDF]
|
 |
|
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.
|
Advertisement
Advertisement
|