help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Biophys. J. BioFAST: First Published June 30, 2006. doi:10.1529/biophysj.105.079343
© 2006 by the Biophysical Society.

A more recent version of this article appeared on September 15, 2006.
This Article
Right arrow Full Text (Rapid PDF)
Right arrow Supplement
Right arrow All Versions of this Article:
biophysj.105.079343v1
91/6/2326    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 Bhattacharya, D.
Right arrow Articles by Shivashankar, G.V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bhattacharya, D.
Right arrow Articles by Shivashankar, G.V.

CELL BIOPHYSICS

EGFP tagged core and linker histones diffuse via distinct mechanisms within living cells

Dipanjan Bhattacharya 1, Aprotim Mazumder 2, Annie Miriam 2 and G.V. Shivashankar 2*

1 Raman Research Institute
2 National Centre for Biological Sciences

* To whom correspondence should be addressed. E-mail: shiva{at}ncbs.res.in.

Submitted on December 13, 2005
Revised on January 16, 2006
Accepted on 9 June 2006


  Abstract
The effect of chromatin organization on EGFP tagged histone protein dynamics within the cell nucleus has been probed using fluorescence correlation and recovery measurements on single living Hela cells. Our studies reveal that free fraction of core-particle histones exist as multimers within the cell nucleus while the linker histones exist in monomeric forms. The multimeric state of core histones is found to be invariant across mammalian and polytene chromosomes and this is ATP dependent. In contrast, the dynamics of the linker histones exhibits two distinct diffusion timescales corresponding to its transient binding and unbinding to chromatin governed by the tail domain residues. Under conditions of chromatin condensation induced by apoptosis, the free multimeric fraction of core histones is found to become immobile, while the monomeric linker histone mobility is partially reduced. In addition, we observe differences in nuclear co-localization of linker and core particle histones. These results are validated through Brownian dynamics simulation of core and linker histone mobility. Our findings provide a framework to understand the coupling between the state of chromatin assembly and histone protein dynamics that is central to accessing regulatory sites on the genome.

Key Words: FCS, FRAP, chromatin assembly, diffusion, histones, single cell biophysics




This article has been cited by other articles:


Home page
 Biophys. JHome page
A. Mazumder, T. Roopa, A. Basu, L. Mahadevan, and G. V. Shivashankar
Dynamics of Chromatin Decondensation Reveals the Structural Integrity of a Mechanically Prestressed Nucleus
Biophys. J., September 15, 2008; 95(6): 3028 - 3035.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
J. P. Skinner, Y. Chen, and J. D. Muller
Fluorescence Fluctuation Spectroscopy in the Presence of Immobile Fluorophores
Biophys. J., March 15, 2008; 94(6): 2349 - 2360.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2006 by the Biophysical Society.