JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 QUICK SEARCH:   [advanced]


     


A more recent version of this article appeared on January 12, 2007
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
282/2/1018    most recent
M609473200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
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 Google Scholar
Google Scholar
Right arrow Articles by Ulyanova, N. P.
Right arrow Articles by Schnitzler, G. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ulyanova, N. P.
Right arrow Articles by Schnitzler, G. R.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print November 22, 2006
J. Biol. Chem, 10.1074/jbc.M609473200
Submitted on October 6, 2006
Revised on November 14, 2006
Accepted on November 20, 2006

Inverted factor access and slow reversion characterize SWI/SNF-altered nucleosome dimers

Natalia P. Ulyanova and Gavin R. Schnitzler

Biochemistry, Tufts University School of Medicine, Boston, MA 02111

Corresponding Author: gavin.schnitzler{at}tufts.edu

Human SWI/SNF is an ATP-dependent chromatin remodeling complex with important functions in activation and repression of cellular genes. Previously, we showed that hSWI/SNF creates structurally-altered dimers from mononucleosome cores. More recently we found that hSWI/SNF also generates abundant structurally-altered dinucleosomes, called altosomes, on polynucleosomal templates. Here, we find that dimers revert to normal nucleosomes at a similar rate as altosomes and can also be cleaved to yield nucleosomal particles with mobilities similar to mononucleosomes. Using these and other shared properties we propose a single model for both types of hSWI/SNF product. In addition, we further characterize the accessibility of altered dimers to transcription factors, and find that the DNA in dimers is most accessible in the middle and least accessible at the ends, directly opposite the profile of normal mononucleosomes. We also find that transcription factor binding can influence the ratio of normal nucleosomes and dimers as hSWI/SNF products. Implications for the interplay between hSWI/SNF products and transcription factors are discussed.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?





HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.