This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bloch, D. B.
Right arrow Articles by Bloch, K. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bloch, D. B.
Right arrow Articles by Bloch, K. D.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, August 2000, p. 6138-6146, Vol. 20, No. 16
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Sp110 Localizes to the PML-Sp100 Nuclear Body and May Function as a Nuclear Hormone Receptor Transcriptional Coactivator

Donald B. Bloch,1,2,* Ayako Nakajima,1,2 Tod Gulick,1,3 Jean-Daniel Chiche,1,4 Donald Orth,1,2 Suzanne M. de la Monte,1,5 and Kenneth D. Bloch1,4

Department of Medicine, Harvard Medical School,1 and Arthritis Unit,2 Diabetes Research Center,3 Cardiovascular Research Center and Cardiology Division, General Medical Services,4 and Division of Neuropathology and Cancer Center,5 Massachusetts General Hospital, Boston, Massachusetts

Received 27 January 2000/Returned for modification 8 March 2000/Accepted 16 May 2000

The nuclear body is a multiprotein complex that may have a role in the regulation of gene transcription. This structure is disrupted in a variety of human disorders including acute promyelocytic leukemia and viral infections, suggesting that alterations in the nuclear body may have an important role in the pathogenesis of these diseases. In this study, we identified a cDNA encoding a leukocyte-specific nuclear body component designated Sp110. The N-terminal portion of Sp110 was homologous to two previously characterized components of the nuclear body (Sp100 and Sp140). The C-terminal region of Sp110 was homologous to the transcription intermediary factor 1 (TIF1) family of proteins. High levels of Sp110 mRNA were detected in human peripheral blood leukocytes and spleen but not in other tissues. The levels of Sp110 mRNA and protein in the human promyelocytic leukemia cell line NB4 increased following treatment with all-trans retinoic acid (ATRA), and Sp110 localized to PML-Sp100 nuclear bodies in ATRA-treated NB4 cells. Because of the structural similarities between Sp110 and TIF1 proteins, the effect of Sp110 on gene transcription was examined. An Sp110 DNA-binding domain fusion protein activated transcription of a reporter gene in transfected mammalian cells. In addition, Sp110 produced a marked increase in ATRA-mediated expression of a reporter gene containing a retinoic acid response element. Taken together, the results of this study demonstrate that Sp110 is a member of the Sp100/Sp140 family of nuclear body components and that Sp110 may function as a nuclear hormone receptor transcriptional coactivator. The predominant expression of Sp110 in leukocytes and the enhanced expression of Sp110 in NB4 cells treated with ATRA raise the possibility that Sp110 has a role in inducing differentiation of myeloid cells.

* Corresponding author. Mailing address: Massachusetts General Hospital-East, CNY 149 13th St., Charlestown, MA 02129. Phone: (617) 726-3780. Fax: (617) 726-5651. E-mail: bloch{at}helix.mgh.harvard.edu.

Molecular and Cellular Biology, August 2000, p. 6138-6146, Vol. 20, No. 16
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Marquis, J.-F., LaCourse, R., Ryan, L., North, R. J., Gros, P. (2009). Genetic and Functional Characterization of the Mouse Trl3 Locus in Defense against Tuberculosis. J. Immunol. 182: 3757-3767 [Abstract] [Full Text]  
  • Calderwood, M. A., Venkatesan, K., Xing, L., Chase, M. R., Vazquez, A., Holthaus, A. M., Ewence, A. E., Li, N., Hirozane-Kishikawa, T., Hill, D. E., Vidal, M., Kieff, E., Johannsen, E. (2007). Epstein-Barr virus and virus human protein interaction maps. Proc. Natl. Acad. Sci. USA 104: 7606-7611 [Abstract] [Full Text]  
  • Warren, E. H., Vigneron, N. J., Gavin, M. A., Coulie, P. G., Stroobant, V., Dalet, A., Tykodi, S. S., Xuereb, S. M., Mito, J. K., Riddell, S. R., Van den Eynde, B. J. (2006). An antigen produced by splicing of noncontiguous peptides in the reverse order.. Science 313: 1444-1447 [Abstract] [Full Text]  
  • Tosh, K., Campbell, S. J., Fielding, K., Sillah, J., Bah, B., Gustafson, P., Manneh, K., Lisse, I., Sirugo, G., Bennett, S., Aaby, P., McAdam, K. P. W. J., Bah-Sow, O., Lienhardt, C., Kramnik, I., Hill, A. V. S. (2006). Variants in the SP110 gene are associated with genetic susceptibility to tuberculosis in West Africa. Proc. Natl. Acad. Sci. USA 103: 10364-10368 [Abstract] [Full Text]  
  • Thye, T, Browne, E N, Chinbuah, M A, Gyapong, J, Osei, I, Owusu-Dabo, E, Niemann, S, Rusch-Gerdes, S, Horstmann, R D, Meyer, C G (2006). No associations of human pulmonary tuberculosis with Sp110 variants.. J. Med. Genet. 43: e32-e32 [Abstract] [Full Text]  
  • French, P. J., Swagemakers, S. M.A., Nagel, J. H.A., Kouwenhoven, M. C.M., Brouwer, E., van der Spek, P., Luider, T. M., Kros, J. M., van den Bent, M. J., Sillevis Smitt, P. A. (2005). Gene Expression Profiles Associated with Treatment Response in Oligodendrogliomas. Cancer Res. 65: 11335-11344 [Abstract] [Full Text]  
  • Ching, R. W., Dellaire, G., Eskiw, C. H., Bazett-Jones, D. P. (2005). PML bodies: a meeting place for genomic loci?. J. Cell Sci. 118: 847-854 [Abstract] [Full Text]  
  • Nicewonger, J., Suck, G., Bloch, D., Swaminathan, S. (2004). Epstein-Barr Virus (EBV) SM Protein Induces and Recruits Cellular Sp110b To Stabilize mRNAs and Enhance EBV Lytic Gene Expression. J. Virol. 78: 9412-9422 [Abstract] [Full Text]  
  • Yu, J. H., Nakajima, A., Nakajima, H., Diller, L. R., Bloch, K. D., Bloch, D. B. (2004). Restoration of Promyelocytic Leukemia Protein-Nuclear Bodies in Neuroblastoma Cells Enhances Retinoic Acid Responsiveness. Cancer Res. 64: 928-933 [Abstract] [Full Text]  
  • Watashi, K., Hijikata, M., Tagawa, A., Doi, T., Marusawa, H., Shimotohno, K. (2003). Modulation of Retinoid Signaling by a Cytoplasmic Viral Protein via Sequestration of Sp110b, a Potent Transcriptional Corepressor of Retinoic Acid Receptor, from the Nucleus. Mol. Cell. Biol. 23: 7498-7509 [Abstract] [Full Text]  
  • Surdo, P. L., Bottomley, M. J., Sattler, M., Scheffzek, K. (2003). Crystal Structure and Nuclear Magnetic Resonance Analyses of the SAND Domain from Glucocorticoid Modulatory Element Binding Protein-1 Reveals Deoxyribonucleic Acid and Zinc Binding Regions. Mol. Endocrinol. 17: 1283-1295 [Abstract] [Full Text]  
  • Madani, N., Millette, R., Platt, E. J., Marin, M., Kozak, S. L., Bloch, D. B., Kabat, D. (2002). Implication of the Lymphocyte-Specific Nuclear Body Protein Sp140 in an Innate Response to Human Immunodeficiency Virus Type 1. J. Virol. 76: 11133-11138 [Abstract] [Full Text]  
  • Wasylyk, C., Schlumberger, S. E., Criqui-Filipe, P., Wasylyk, B. (2002). Sp100 Interacts with ETS-1 and Stimulates Its Transcriptional Activity. Mol. Cell. Biol. 22: 2687-2702 [Abstract] [Full Text]  
  • Seeler, J.-S., Marchio, A., Losson, R., Desterro, J. M. P., Hay, R. T., Chambon, P., Dejean, A. (2001). Common Properties of Nuclear Body Protein SP100 and TIF1{alpha} Chromatin Factor: Role of SUMO Modification. Mol. Cell. Biol. 21: 3314-3324 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»