Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
 QUICK SEARCH:   [advanced]


     


MBC in Press, published online ahead of print February 8, 2006
Mol. Biol. Cell 10.1091/mbc.E05-11-1063

A more recent version of this article appeared on April 1, 2006
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E05-11-1063v1
17/4/1711    most recent
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Moorefield, K. S.
Right arrow Articles by Horowitz, J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moorefield, K. S.
Right arrow Articles by Horowitz, J. M.

Submitted on November 18, 2005
Revised on January 25, 2006
Accepted on February 2, 2006

Sp2 Localizes to Subnuclear Foci Associated with the Nuclear Matrix

K. Scott Moorefield,* Haifeng Yin,* Teresa D. Nichols,{dagger} Christopher Cathcart,{ddagger} Steven O. Simmons,{sect} and Jonathan M. Horowitz{dagger}

Graduate Programs in *Genomic Sciences and {sect}Toxicology and the {dagger}Department of Molecular Biomedical Sciences, College of Veterinary Medicine, North Carolina State University, Raleigh, NC 27606; {ddagger}Nikon Instruments, Melville, NY 11747

Monitoring Editor: William Tansey

We have reported that extracts prepared from many human and mouse cell lines show little or no Sp2 DNA-binding activity, and that Sp2 has little or no capacity to stimulate transcription of promoters that are activated by Sp1, Sp3, and Sp4. Using an array of chimeric Sp1/Sp2 proteins we showed further that Sp2 DNA-binding activity and trans-activation are each negatively regulated in mammalian cells. As part of an ongoing effort to study Sp2 function and regulation we characterized its subcellular localization in comparison with other Sp-family members in fixed and live cells. We report that (i) Sp2 localizes largely within subnuclear foci associated with the nuclear matrix, and (ii) these foci are distinct from promyelocytic oncogenic domains and appear to be stable during an 18 h time course of observation. Deletion analyses identified a 37 amino acid sequence spanning the first zinc-"finger" that is sufficient to direct nuclear matrix association, and this region also encodes a bipartite nuclear localization sequence. A second nuclear matrix targeting sequence is encoded within the Sp2 trans-activation domain. We conclude that Sp2 preferentially associates with the nuclear matrix and speculate that this subcellular localization plays an important role in the regulation of Sp2 function.


Address correspondence to: Jonathan M. Horowitz (jon_horowitz{at}ncsu.edu)




This article has been cited by other articles:


Home page
J. Cell Sci.Home page
J. F.-X. Ainscough, F. A. Rahman, H. Sercombe, A. Sedo, B. Gerlach, and D. Coverley
C-terminal domains deliver the DNA replication factor Ciz1 to the nuclear matrix
J. Cell Sci., January 1, 2007; 120(1): 115 - 124.
[Abstract] [Full Text] [PDF]




Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2006 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.