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Takahiro Goshima, Midori Shimada, Jafar Sharif, Hiromi Matsuo, Toshinori Misaki, Yoshikazu Johmura, Kazuhiro Murata, Haruhiko Koseki, Makoto Nakanishi
Histone variants play specific roles in maintenance and regulation of chromatin structures. H2ABbd, an H2A variant, possesses a highly divergent structure compared with canonical H2A and is highly expressed in postmeiotic germ cells, but its functions in the regulation of gene expression are largely unknown. In the present study, we investigated the cellular phenotype associated with enforced H2ABbd expression. Among H2A variants, H2ABbd specifically caused growth defect in human cells and induced apoptosis...
April 25, 2014: Journal of Biological Chemistry
Margaret L Shaw, Evan J Williams, Susan Hawes, Richard Saffery
Recent studies, primarily in mouse embryonic stem cells, have highlighted the unique chromatin state of pluripotent stem cells, including the incorporation of histone variants into specific genomic locations, and its role in facilitating faithful expression of genes during development. However, there is little information available on the expression and subcellular localisation of histone variants in human embryonic stem cells (hESCs). In this study, we confirmed the expression of a panel of histone variant genes in several hESC lines and demonstrated the utility of transfection of in vitro transcribed, epitope-tagged mRNAs to characterise the subcellular localisation of these proteins...
December 2009: Molecular Reproduction and Development
Emily Bernstein, Tara L Muratore-Schroeder, Robert L Diaz, Jennifer C Chow, Lakshmi N Changolkar, Jeffrey Shabanowitz, Edith Heard, John R Pehrson, Donald F Hunt, C David Allis
Histone variants play an important role in numerous biological processes through changes in nucleosome structure and stability and possibly through mechanisms influenced by posttranslational modifications unique to a histone variant. The family of histone H2A variants includes members such as H2A.Z, the DNA damage-associated H2A.X, macroH2A (mH2A), and H2ABbd (Barr body-deficient). Here, we have undertaken the challenge to decipher the posttranslational modification-mediated "histone code" of mH2A, a variant generally associated with certain forms of condensed chromatin such as the inactive X chromosome in female mammals...
February 5, 2008: Proceedings of the National Academy of Sciences of the United States of America
Dimitar Angelov, Vladimir A Bondarenko, Sébastien Almagro, Hervé Menoni, Fabien Mongélard, Fabienne Hans, Flore Mietton, Vasily M Studitsky, Ali Hamiche, Stefan Dimitrov, Philippe Bouvet
Remodeling machines play an essential role in the control of gene expression, but how their activity is regulated is not known. Here we report that the nuclear protein nucleolin possesses a histone chaperone activity and that this factor greatly enhances the activity of the chromatin remodeling machineries SWI/SNF and ACF. Interestingly, nucleolin is able to induce the remodeling by SWI/SNF of macroH2A, but not of H2ABbd nucleosomes, which are otherwise resistant to remodeling. This new histone chaperone promotes the destabilization of the histone octamer, helping the dissociation of a H2A-H2B dimer, and stimulates the SWI/SNF-mediated transfer of H2A-H2B dimers...
April 19, 2006: EMBO Journal
Dimitar Angelov, André Verdel, Woojin An, Vladimir Bondarenko, Fabienne Hans, Cécile-Marie Doyen, Vassily M Studitsky, Ali Hamiche, Robert G Roeder, Philippe Bouvet, Stefan Dimitrov
A histone variant H2ABbd was recently identified, but its function is totally unknown. Here we have studied the structural and functional properties of nucleosome and nucleosomal arrays reconstituted with this histone variant. We show that H2ABbd can replace the conventional H2A in the nucleosome, but this replacement results in alterations of the nucleosomal structure. The remodeling complexes SWI/SNF and ACF are unable to mobilize the variant H2ABbd nucleosome. However, SWI/SNF was able to increase restriction enzyme access to the variant nucleosome and assist the transfer of variant H2ABbd-H2B dimer to a tetrameric histone H3-H4 particle...
October 1, 2004: EMBO Journal
Thierry Gautier, D Wade Abbott, Annie Molla, Andre Verdel, Juan Ausio, Stefan Dimitrov
The histone H2ABbd is a novel histone variant of H2A with a totally unknown function. We have investigated the behaviour of the H2ABbd nucleosomes. Nucleosomes were reconstituted with recombinant histone H2ABbd and changes in their conformations at different salt concentrations were studied by analytical centrifugation. The data are in agreement with H2ABbd being less tightly bound compared with conventional H2A in the nucleosome. In addition, stable cell lines expressing either green fluorescent protein (GFP)-H2A or GFP-H2ABbd were established and the mobility of both fusions was measured by fluorescence recovery after photobleaching...
July 2004: EMBO Reports
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