Journal ArticleDOI
Dynamic binding of histone H1 to chromatin in living cells
Reads0
Chats0
TLDR
The results support a model in which linker histones bind dynamically to chromatin in a stop-and-go mode, suggesting a higher rate of exchange upon chromatin remodelling.Abstract:
The linker histone H1 is believed to be involved in chromatin organization by stabilizing higher-order chromatin structure. Histone H1 is generally viewed as a repressor of transcription as it prevents the access of transcription factors and chromatin remodelling complexes to DNA. Determining the binding properties of histone H1 to chromatin in vivo is central to understanding how it exerts these functions. We have used photobleaching techniques to measure the dynamic binding of histone H1-GFP to unperturbed chromatin in living cells. Here we show that almost the entire population of H1-GFP is bound to chromatin at any one time; however, H1-GFP is exchanged continuously between chromatin regions. The residence time of H1-GFP on chromatin between exchange events is several minutes in both euchromatin and heterochromatin. In addition to the mobile fraction, we detected a kinetically distinct, less mobile fraction. After hyperacetylation of core histones, the residence time of H1-GFP is reduced, suggesting a higher rate of exchange upon chromatin remodelling. These results support a model in which linker histones bind dynamically to chromatin in a stop-and-go mode.read more
Citations
More filters
Journal ArticleDOI
Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
TL;DR: It is reported that Hmgb1-/- necrotic cells have a greatly reduced ability to promote inflammation, which proves that the release of HMGB1 can signal the demise of a cell to its neighbours, and cells undergoing apoptosis are programmed to withhold the signal that is broadcast by cells that have been damaged or killed by trauma.
Journal ArticleDOI
Opening of Compacted Chromatin by Early Developmental Transcription Factors HNF3 (FoxA) and GATA-4
TL;DR: The ability of HNF3 to open chromatin is mediated by a high affinity DNA binding site and by the C-terminal domain of the protein, which binds histones H3 and H4.
Journal ArticleDOI
γ-H2AX in recognition and signaling of DNA double-strand breaks in the context of chromatin
TL;DR: The role of γ-H2AX in DNA damage response in the context of chromatin is reviewed and the use of this modification as a surrogate marker for mechanistic studies of DSB induction and processing is discussed.
Journal ArticleDOI
Hyperdynamic Plasticity of Chromatin Proteins in Pluripotent Embryonic Stem Cells
Eran Meshorer,Dhananjay Yellajoshula,Eric M. George,Peter J. Scambler,David T. Brown,Tom Misteli +5 more
TL;DR: It is suggested that hyperdynamic binding of structural chromatin proteins is a functionally important hallmark of pluripotent ES cells that contributes to the maintenance of plasticity in undifferentiated ES cells and to establishing higher-order chromatin structure.
Journal ArticleDOI
How do site‐specific DNA‐binding proteins find their targets?
Stephen E. Halford,John F. Marko +1 more
TL;DR: A simplified version of the 'facilitated diffusion' model of Berg, Winter and von Hippel is presented, showing how non-specific DNA-protein interactions may account for accelerated targeting, by permitting the protein to sample many binding sites per DNA encounter.
References
More filters
Journal ArticleDOI
The language of covalent histone modifications.
Brian D. Strahl,C D Allis +1 more
TL;DR: It is proposed that distinct histone modifications, on one or more tails, act sequentially or in combination to form a ‘histone code’ that is, read by other proteins to bring about distinct downstream events.
Journal ArticleDOI
Histone acetylation in chromatin structure and transcription
TL;DR: The amino termini of histones extend from the nucleosomal core and are modified by acetyltransferases and deacetylases during the cell cycle, which may direct histone assembly and help regulate the unfolding and activity of genes.
Journal ArticleDOI
Histone acetylation and transcriptional regulatory mechanisms
TL;DR: Understanding of the causal relationship between histone acetylation and gene expression has been enhanced dramatically by the identification of proteins with intrinsic hist one acetylase and deacetylase activity, which led to a major paradigm shift in understanding of chromatin structure and transcription regulation.
Journal ArticleDOI
High mobility of proteins in the mammalian cell nucleus
Robert D. Phair,Tom Misteli +1 more
TL;DR: It is shown that many nuclear proteins roam the cell nucleus in vivo and that nuclear compartments are the reflection of the steady-state association/dissociation of its ‘residents’ with the nucleoplasmic space.
Journal ArticleDOI
A direct link between core histone acetylation and transcriptionally active chromatin.
TL;DR: The results demonstrate directly that transcriptionally active genes carry acetylated core histones in chromatin fragments fractions from the nuclei of 15‐day chicken embryo erythrocytes.
Related Papers (5)
Kinetics of Core Histones in Living Human Cells: Little Exchange of H3 and H4 and Some Rapid Exchange of H2b
Hiroshi Kimura,Peter R. Cook +1 more