The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core

Lee, Kyu-Min; Hayes, Jeffrey J.

doi:10.1073/pnas.94.17.8959

Cited by 66 publications

(73 citation statements)

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“…This position is located at the junction of the H2A N-terminal tail and the histone fold domain, near the inside of the superhelical DNA gyre, and therefore is less likely to participate in inter-nucleosomal DNA binding (3,(5)(6)(7)58). Previous experiments have shown that irradiation of mononucleosomes containing H2A-A12C-APB results in crosslinks to DNA located ϳ40 bp to either side of the nucleosome dyad, consistent with the known structure of this complex (3,19). Similar to the previous experiment the HindIII end of nucleosome 1 in the dinucleosome was radiolabled, and H2A-A12C-APB was incorporated into nucleosome 2.…”

Section: Resultsmentioning

confidence: 51%

“…The proteins were checked by SDS-PAGE and trial reconstitutions. APB modification of H2A-G2C, H2B-2C, H3-T6C, and H4-G6C was carried out as previously described (19,55).…”

Section: Preparation Of Native and Apb-modified Histones-recombinantmentioning

confidence: 99%

“…wild type and mutant H2A, H2B, H2A-G2C, and H2B-2C were prepared and purified as preformed dimers as described (19,53). Coding sequences for Xenopus H3-T6C/C110A (containing cysteine and alanine codon substitutions at amino acid positions 6 and 110, respectively) and H4-G6C (containing a cysteine codon at position 6) were constructed and cloned into pET3 expression plasmids.…”

Section: Preparation Of Native and Apb-modified Histones-recombinantmentioning

confidence: 99%

“…In addition, evidence suggests that these domains also participate in protein-protein interactions between histones in the fully condensed chromatin fiber (3,7,16). Despite the perception of the tails as being "unstructured," biochemical and biophysical studies indicate they adopt defined structures and make specific interactions in chromatin (17)(18)(19)(20). The tail domains are not required for assembling or maintaining the structure of the nucleosome core and removal of the tails results in only marginal changes in the hydrodynamic shape, stability, and DNA wrapping within the nucleosome (21)(22)(23).…”

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confidence: 99%

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Intra- and Inter-nucleosomal Protein-DNA Interactions of the Core Histone Tail Domains in a Model System

Zheng

Hayes

2003

Journal of Biological Chemistry

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The core histone tail domains are key regulators of eukaryotic chromatin structure and function and alterations in the tail-directed folding of chromatin fibers and higher order structures are the probable outcome of much of the post-translational modifications occurring in these domains. The functions of the tail domains are likely to involve complex intra-and inter-nucleosomal histone-DNA interactions, yet little is known about either the structures or interactions of these domains. Here we introduce a method for examining inter-nucleosome interactions of the tail domains in a model dinucleosome and determine the propensity of each of the four N-terminal tail domains to mediate such interactions in this system. Using a strong nucleosome "positioning" sequence, we reconstituted a nucleosome containing a single histone site specifically modified with a photoinducible cross-linker within the histone tail domain, and a second nucleosome containing a radiolabeled DNA template. These two nucleosomes were then ligated together and cross-linking induced by brief UV irradiation under various solution conditions. After cross-linking, the two templates were again separated so that cross-linking representing inter-nucleosomal histone-DNA interactions could be unambiguously distinguished from intra-nucleosomal cross-links. Our results show that the N-terminal tails of H2A and H2B, but not of H3 and H4, make internucleosomal histone-DNA interactions within the dinucleosome. The relative extent of intra-to inter-nucleosome interactions was not strongly dependent on ionic strength. Additionally, we find that binding of a linker histone to the dinucleosome increased the association of the H3 and H4 tails with the linker DNA region.

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Section: Resultsmentioning

confidence: 51%

“…The proteins were checked by SDS-PAGE and trial reconstitutions. APB modification of H2A-G2C, H2B-2C, H3-T6C, and H4-G6C was carried out as previously described (19,55).…”

Section: Preparation Of Native and Apb-modified Histones-recombinantmentioning

confidence: 99%

Section: Preparation Of Native and Apb-modified Histones-recombinantmentioning

confidence: 99%

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confidence: 99%

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Intra- and Inter-nucleosomal Protein-DNA Interactions of the Core Histone Tail Domains in a Model System

Zheng

Hayes

2003

Journal of Biological Chemistry

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“…Nucleosome Reconstitution-Recombinant Xenopus H2A and the cysteine-substituted mutant H2BG26C were prepared as preformed dimers, and the latter was modified with 4-azidophenacyl bromide (APB, 2 Sigma) as described (37,38). Histone H3/H4 tetramers were prepared from chicken erythrocyte nuclei, and nucleosomes were reconstituted with either native H2A/H2B or H2A/H2BG26C-APB.…”

Section: Methodsmentioning

confidence: 99%

Nucleosome Sliding Induced by the xMi-2 Complex Does Not Occur Exclusively via a Simple Twist-diffusion Mechanism

Wade

Hayes

2003

Journal of Biological Chemistry

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ATP-dependent chromatin remodeling complexes can induce the translocation (sliding) of nucleosomes in cis along DNA, but the mechanism by which sliding occurs is not well defined. We previously presented evidence that sliding induced by the human SWI/SNF complex does not occur solely via a proposed "twist-diffusion" mechanism whereby the DNA rotates about its helical axis without displacement from the surface of the nucleosome (Aoyagi, S., and Hayes, J. J. (2002) Mol. Cell. Biol. 22, 7484 -7490). Here we examined whether the Xenopus Mi-2 nucleosome remodeling complex induces nucleosome sliding via a twist-diffusion mechanism with nucleosomes assembled onto DNA templates containing branched DNA structures expected to sterically hinder rotation of the DNA helix on the nucleosome surface. We find that the branched DNA-containing nucleosomes undergo xMi-2-catalyzed sliding at a rate and extent identical to that of nucleosomes assembled on native DNA fragments. These results indicate that both the hSWI/ SNF and xMi-2 complexes induce nucleosome sliding via a mechanism(s) other than simple twist diffusion and are consistent with models in which the DNA largely maintains its rotational orientation with respect to the histone surface.In the nucleus, the eukaryotic genome is packaged in the form of a highly condensed chromatin fiber through its interactions with histones and non-histone proteins (1, 2). To allow efficient progression of nuclear processes, cells have developed several mechanisms to facilitate access of DNA target sites within chromatin by trans-acting factors (3-5). One strategy involves targeted post-translational modifications of histone proteins such as acetylation, methylation, and phosphorylation that may directly alter the biochemical properties of chromatin or signal binding and recruitment of ancillary factors (6 -10). A second strategy involves the activity of ATP-dependent chromatin remodeling complexes that couple the energy derived from ATP hydrolysis to alter chromatin structure, facilitating the activity of trans-acting factors (4, 11-13).All ATP-dependent chromatin remodeling complexes contain a subunit that belongs to the SNF2 superfamily of ATPases (14). There are four main classes within this superfamily, differentiated by homology to the SWI2/SNF2, ISWI, INO80, and Mi-2 ATPase subunits within these complexes (11)(12)(13)15). The molecular mechanism of nucleosome remodeling by the ATPdependent chromatin remodeling complexes has been under intense study. Remodeling complexes such as the SWI/SNF complex have been shown to cause disruption of histone-DNA interactions as detected by electron energy loss microscopy and atomic force microscopy studies (16,17). The loss of histone-DNA interactions within the nucleosome is correlated with the increase in activities of various transcription factors, restriction enzymes, and DNase I on nucleosomal DNA (18 -21). Evidence indicates that Mi-2 complexes also cause such disruptions in histone-DNA interactions as detected by increase in accessibility to...

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Arm-domain interactions in proteins: a review

Schleif¹

1999

Proteins

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The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core

Cited by 66 publications

References 44 publications

Intra- and Inter-nucleosomal Protein-DNA Interactions of the Core Histone Tail Domains in a Model System

Intra- and Inter-nucleosomal Protein-DNA Interactions of the Core Histone Tail Domains in a Model System

Nucleosome Sliding Induced by the xMi-2 Complex Does Not Occur Exclusively via a Simple Twist-diffusion Mechanism

Arm-domain interactions in proteins: a review

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