The core histone tail domains contribute to sequence-dependent nucleosome positioning.

@article{citeulike:1082418, abstract = {The precise positioning of nucleosomes plays a critical role in the regulation of gene expression by modulating the DNA binding activity of trans-acting factors. However, molecular determinants responsible for positioning are not well understood. We examined whether the removal of the core histone tail domains from nucleosomes reconstituted with specific DNA fragments led to alteration of translational positions. Remarkably, we find that removal of tail domains from a nucleosome assembled on a DNA fragment containing a Xenopus borealis somatic-type 5S RNA gene results in repositioning of nucleosomes along the DNA, including two related major translational positions that move about 20bp further upstream with respect to the 5S gene. In a nucleosome reconstituted with a DNA fragment containing the promoter of a Drosophila alcohol dehydrogenase gene, several translational positions shifted by about 10bp along the DNA upon tail removal. However, the positions of nucleosomes assembled with a DNA fragment known to have one of the highest binding affinities for core histone proteins in the mouse genome were not altered by removal of core histone tail domains. Our data support the notion that the basic tail domains bind to nucleosomal DNA and influence the selection of translational position of nucleosomes and that once tails are removed movement between translational positions occurs in a facile manner on some sequences. However, the effect of the N-terminal tails on the positioning and movement of a nucleosome appears to be dependent on the DNA sequence such that the contribution of the tails can be masked by very high-affinity DNA sequences. Our results suggest a mechanism whereby sequence-dependent nucleosome positioning can be specifically altered by regulated changes in histone tail-DNA interactions in chromatin.}, address = {Department of Biochemistry and Biophysics, University of Rochester; School of Medicine and Dentistry; Medical Center 3-6710, Rochester, NY 14642.}, author = {Yang, Zungyoon and Zheng, Chunyang and Hayes, Jeffrey J J. }, citeulike-article-id = {1082418}, doi = {10.1074/jbc.M610584200}, issn = {0021-9258}, journal = {J Biol Chem}, keywords = {histone, nucleosome, sequence\_specificity}, month = {January}, posted-at = {2007-02-01 19:34:26}, priority = {2}, title = {The core histone tail domains contribute to sequence-dependent nucleosome positioning.}, url = {http://dx.doi.org/10.1074/jbc.M610584200}, year = {2007} }

TY - JOUR ID - citeulike:1082418 L3 - citeulike-article-id:1082418 TI - The core histone tail domains contribute to sequence-dependent nucleosome positioning. JF - J Biol Chem AD - Department of Biochemistry and Biophysics, University of Rochester; School of Medicine and Dentistry; Medical Center 3-6710, Rochester, NY 14642. SN - 0021-9258 N2 - The precise positioning of nucleosomes plays a critical role in the regulation of gene expression by modulating the DNA binding activity of trans-acting factors. However, molecular determinants responsible for positioning are not well understood. We examined whether the removal of the core histone tail domains from nucleosomes reconstituted with specific DNA fragments led to alteration of translational positions. Remarkably, we find that removal of tail domains from a nucleosome assembled on a DNA fragment containing a Xenopus borealis somatic-type 5S RNA gene results in repositioning of nucleosomes along the DNA, including two related major translational positions that move about 20bp further upstream with respect to the 5S gene. In a nucleosome reconstituted with a DNA fragment containing the promoter of a Drosophila alcohol dehydrogenase gene, several translational positions shifted by about 10bp along the DNA upon tail removal. However, the positions of nucleosomes assembled with a DNA fragment known to have one of the highest binding affinities for core histone proteins in the mouse genome were not altered by removal of core histone tail domains. Our data support the notion that the basic tail domains bind to nucleosomal DNA and influence the selection of translational position of nucleosomes and that once tails are removed movement between translational positions occurs in a facile manner on some sequences. However, the effect of the N-terminal tails on the positioning and movement of a nucleosome appears to be dependent on the DNA sequence such that the contribution of the tails can be masked by very high-affinity DNA sequences. Our results suggest a mechanism whereby sequence-dependent nucleosome positioning can be specifically altered by regulated changes in histone tail-DNA interactions in chromatin. KW - histone KW - nucleosome KW - sequence_specificity AU - Yang, Zungyoon AU - Zheng, Chunyang AU - Hayes, Jeffrey J PY - 2007/01/17/ UR - http://dx.doi.org/10.1074/jbc.M610584200 ER -