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Please use this identifier to cite or link to this item: http://hdl.handle.net/2289/3330

Title: EGFP-Tagged Core and Linker Histones Diffuse via Distinct Mechanisms within Living Cells
Authors: Bhattacharya, D.
Mazumder, Aprotim
Miriam, S. Annie
Shivashankar, G.V.
Issue Date: Jun-2006
Publisher: Biophysical Society
Citation: Biophysical Journal, 2006, V91, p2326-2336.
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 whereas 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 colocalization 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.
Description: Restricted Access. Please click on the alternative location for the open access full-text.
URI: http://hdl.handle.net/2289/3330
ISSN: E-ISSN: 1542-0086
P-ISSN: 0006-3495
Alternative Location: http://dx.doi.org/10.1529/biophysj.105.079343
Copyright: 2006 The Biophysical Society
Appears in Collections:Research Papers (SCM)

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