| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Papers In Press, published online ahead of print January 15, 2004
Department of Molecular Biomedical Sciences, North Carolina State University, Raleigh, NC 27606
Corresponding Author: jon_horowitz{at}ncsu.edu
Previous studies have indicated that Sp2 binds poorly to GC-rich sequences bound by Sp1 and Sp3, and further functional analyses of Sp2 have been limited. To study Sp2-mediated transcription we employed a PCR-based protocol to determine the Sp2 consensus DNA-binding sequence (5’-GGGCGGGAC-3’), and performed kinetic experiments to show that Sp2 binds this consensus sequence with high affinity (225 pM) in vitro. To determine the functional consequence of Sp2’s interaction with this sequence in vivo, we transformed well-characterized Sp-binding sites within the DHFR promoter to consensus Sp2-binding sites. Incorporation of Sp2-binding sites within the DHFR promoter increased Sp2-mediated trans-activation in transient co-transfection experiments but also revealed Sp2 to be a relatively weak trans-activator with little or no capacity for additive or synergistic trans-activation. Using chimeric molecules prepared with portions of Sp1 and Sp2 and the human prostate specific antigen (PSA) promoter, we show that Sp2 DNA-binding activity and trans-activation are negatively regulated in mammalian cells. Taken together our data indicate that Sp2 is functionally distinct relative to other Sp-family members, and suggests that Sp2 may play a unique role in cell physiology.
J. Biol. Chem, 10.1074/jbc.M313589200
Submitted on December 11, 2003
Revised on January 14, 2004
Accepted on January 15, 2004
Sp2 DNA-binding activity and trans-activation are negatively regulated in mammalian cells
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  M. O. Boylan, L. I. Jepeal, and M. M. Wolfe Sp1/Sp3 binding is associated with cell-specific expression of the glucose-dependent insulinotropic polypeptide receptor gene Am J Physiol Endocrinol Metab, June 1, 2006; 290(6): E1287 - E1295. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. S. Moorefield, H. Yin, T. D. Nichols, C. Cathcart, S. O. Simmons, and J. M. Horowitz Sp2 Localizes to Subnuclear Foci Associated with the Nuclear Matrix Mol. Biol. Cell, April 1, 2006; 17(4): 1711 - 1722. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. W. Vogel, Z. Zhuang, J. Li, H. Okamoto, M. Furuta, Y.-S. Lee, W. Zeng, E. H. Oldfield, A. O. Vortmeyer, and R. J. Weil Proteins and Protein Pattern Differences between Glioma Cell Lines and Glioblastoma Multiforme Clin. Cancer Res., May 15, 2005; 11(10): 3624 - 3632. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. Tsika, J. Ji, and R. Tsika Sp3 Proteins Negatively Regulate {beta} Myosin Heavy Chain Gene Expression during Skeletal Muscle Inactivity Mol. Cell. Biol., December 15, 2004; 24(24): 10777 - 10791. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
