JBC Connect with Cosmo for Collagen Detection

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


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
Right arrow Citation Map
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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Boyer, L. A.
Right arrow Articles by Peterson, C. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Boyer, L. A.
Right arrow Articles by Peterson, C. L.
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?

J Biol Chem, Vol. 275, Issue 16, 11545-11552, April 21, 2000

Roles of the Histone H2A-H2B Dimers and the (H3-H4)2 Tetramer in Nucleosome Remodeling by the SWI-SNF Complex*

Laurie A. BoyerDagger , Xiao Shao§, Richard H. Ebright§, and Craig L. PetersonDagger

From the Dagger  Program in Molecular Medicine and Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01605 and the § Howard Hughes Medical Institute, Waksman Institute, and Department of Chemistry, Rutgers University, Piscataway, New Jersey 08854

SWI-SNF is an ATP-dependent chromatin remodeling complex required for expression of a number of yeast genes. Previous studies have suggested that SWI-SNF action may remove or rearrange the histone H2A-H2B dimers or induce a novel alteration in the histone octamer. Here, we have directly tested these and other models by quantifying the remodeling activity of SWI-SNF on arrays of (H3-H4)2 tetramers, on nucleosomal arrays reconstituted with disulfide-linked histone H3, and on arrays reconstituted with histone H3 derivatives site-specifically modified at residue 110 with the fluorescent probe acetylethylenediamine-(1,5)-naphthol sulfonate. We find that SWI-SNF can remodel (H3-H4)2 tetramers, although tetramers are poor substrates for SWI-SNF remodeling compared with nucleosomal arrays. SWI-SNF can also remodel nucleosomal arrays that harbor disulfide-linked (H3-H4)2 tetramers, indicating that SWI-SNF action does not involve an obligatory disruption of the tetramer. Finally, we find that although the fluorescence emission intensity of acetylethylenediamine-(1,5)-naphthol sulfonate-modified histone H3 is sensitive to octamer structure, SWI-SNF action does not alter fluorescence emission intensity. These data suggest that perturbation of the histone octamer is not a requirement or a consequence of ATP-dependent nucleosome remodeling by SWI-SNF.


* This work was supported by National Institutes of Health Grant GM49056-07 (to C. L. P.) and by a Howard Hughes Medical Institute investigatorship (to R. H. E.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: 373 Plantation St., Biotech 2, Suite 301, University of Massachusetts Medical School, Worcester, MA 01605. Tel.: 508-856-5858; Fax: 508-856-4289; E-mail: craig.peterson@umassmed.edu.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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?


This article has been cited by other articles:


Home page
Mol. Cell. Biol.Home page
C. L. Smith and C. L. Peterson
A Conserved Swi2/Snf2 ATPase Motif Couples ATP Hydrolysis to Chromatin Remodeling
Mol. Cell. Biol., July 15, 2005; 25(14): 5880 - 5892.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
H. Wang, R. Bash, J. G. Yodh, G. Hager, S. M. Lindsay, and D. Lohr
Using Atomic Force Microscopy to Study Nucleosome Remodeling on Individual Nucleosomal Arrays in Situ
Biophys. J., September 1, 2004; 87(3): 1964 - 1971.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
C. L. Peterson and J. Cote
Cellular machineries for chromosomal DNA repair
Genes & Dev., March 15, 2004; 18(6): 602 - 616.
[Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
S. Aoyagi and J. J. Hayes
hSWI/SNF-Catalyzed Nucleosome Sliding Does Not Occur Solely via a Twist-Diffusion Mechanism
Mol. Cell. Biol., November 1, 2002; 22(21): 7484 - 7490.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. Y. Wu, D. C. Tkachuck, R. S. Roberson, and W. H. Schubach
The Human SNF5/INI1 Protein Facilitates the Function of the Growth Arrest and DNA Damage-inducible Protein (GADD34) and Modulates GADD34-bound Protein Phosphatase-1 Activity
J. Biol. Chem., July 26, 2002; 277(31): 27706 - 27715.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
S. Aoyagi, G. Narlikar, C. Zheng, S. Sif, R. E. Kingston, and J. J. Hayes
Nucleosome Remodeling by the Human SWI/SNF Complex Requires Transient Global Disruption of Histone-DNA Interactions
Mol. Cell. Biol., June 1, 2002; 22(11): 3653 - 3662.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
L. A. Boyer, C. Logie, E. Bonte, P. B. Becker, P. A. Wade, A. P. Wolffe, C. Wu, A. N. Imbalzano, and C. L. Peterson
Functional Delineation of Three Groups of the ATP-dependent Family of Chromatin Remodeling Enzymes
J. Biol. Chem., June 16, 2000; 275(25): 18864 - 18870.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.