JBC

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


     


Originally published In Press as doi:10.1074/jbc.M401805200 on April 13, 2004

J. Biol. Chem., Vol. 279, Issue 24, 25017-25023, June 11, 2004
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
279/24/25017    most recent
M401805200v1
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 Andrin, C.
Right arrow Articles by Hendzel, M. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Andrin, C.
Right arrow Articles by Hendzel, M. J.
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?

F-actin-dependent Insolubility of Chromatin-modifying Components*

Christi Andrin and Michael J. Hendzel{ddagger}

From the Department of Oncology, University of Alberta, Edmonton, Alberta T6G 1Z2, Canada

Many complexes involved in chromatin modification are difficult to isolate and commonly found associated with nuclear matrix preparations. In this study, we examine the elution properties of chromatin-modifying components under different extraction conditions. We find that most, but not all, histone acetyltransferases and histone deacetylases predominantly partition with the nuclear pellet during intermediate salt extraction. In attempts to identify a biological basis for the observed insolubility, we demonstrate that depolymerizing cellular actin, but not cellular tubulin, mobilizes a significant proportion of the insoluble pool into the intermediate salt-soluble nuclear extract. The disruption of cellular F-actin releases a specific subset of high molecular weight, active, nuclear histone deacetylase complexes that are not found under normal conditions. This study demonstrates that actin polymerization, a physiologically relevant process, is responsible for the observed insolubility of these components during nuclear extract preparation and establishes a simple strategy for isolating subsets of chromatin-modifying complexes that are otherwise depleted or absent under the same extraction conditions.


Received for publication, February 18, 2004 , and in revised form, April 8, 2004.

* This work was supported by an operating grant from the Canadian Institutes of Health Research. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} A scholar of the Alberta Heritage Foundation for Medical Research and a Canadian Institutes of Health Research New Investigator. To whom correspondence should be addressed: Rm. 3332, 11560 University Ave., Edmonton, Alberta T6G 1Z2, Canada. Tel.: 780-432-8439; Fax: 780-432-8892; E-mail: michaelh{at}cancerboard.ab.ca.


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. Biol. CellHome page
A. Bronisz, S. M. Sharma, R. Hu, J. Godlewski, G. Tzivion, K. C. Mansky, and M. C. Ostrowski
Microphthalmia-associated Transcription Factor Interactions with 14-3-3 Modulate Differentiation of Committed Myeloid Precursors
Mol. Biol. Cell, September 1, 2006; 17(9): 3897 - 3906.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
E. Cavellan, P. Asp, P. Percipalle, and A.-K. O. Farrants
The WSTF-SNF2h Chromatin Remodeling Complex Interacts with Several Nuclear Proteins in Transcription
J. Biol. Chem., June 16, 2006; 281(24): 16264 - 16271.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
S. He and J. R. Davie
Sp1 and Sp3 foci distribution throughout mitosis
J. Cell Sci., March 15, 2006; 119(6): 1063 - 1070.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Biol.Home page
D. McDonald, G. Carrero, C. Andrin, G. de Vries, and M. J. Hendzel
Nucleoplasmic {beta}-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations.
J. Cell Biol., February 13, 2006; 172(4): 541 - 552.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
T. Pederson and U. Aebi
Nuclear Actin Extends, with No Contraction in Sight
Mol. Biol. Cell, November 1, 2005; 16(11): 5055 - 5060.
[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 © 2004 by the American Society for Biochemistry and Molecular Biology.