286 research outputs found
Allis, D., et. al. / Editor Epigenetics
No full textC. David Allis, editor. Epigenetics
Second edition
The regulation of gene expression in many biological processes involves epigenetic mechanisms. In this new volume, 24 chapters written by experts in the field discuss epigenetic effects from many perspectives. There are chapters on the basic molecular mechanisms underpinning epigenetic regulation, discussion of cellular processes that rely on this kind of regulation, and surveys of organisms in which it has been most studied. Thus, there are chapters on histone and DNA methylation, siRNAs and gene silencing; X-chromosome inactivation, dosage compensation and imprinting; and discussion of epigenetics in microbes, plants, insects, and mammals. The last part of the book looks at how epigenetic mechanisms act in cell division and differentiation, and how errors in these pathways contribute to cancer and other human diseases. Also discussed are consequences of epigenetics in attempts to clone animals. This book is a major resource for those working in the field, as well as being a suitable text for advanced undergraduate and graduate courses on gene regulation.https://digitalcommons.rockefeller.edu/ru-authors/1004/thumbnail.jp
Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A.X is mediated by the protein phosphatase eyes absent
No full textIn mammalian cells, the DNA damage-related histone H2A variant H2A.X is characterized by a C-terminal tyrosyl residue, Tyr-142, that is phosphorylated by an atypical kinase, WSTF. The phosphorylation status of Tyr-142 in H2A.X has been shown to be an important regulator of the DNA damage response by controlling the formation of �H2A.X foci, which are platforms for recruiting molecules involved in DNA damage repair and signaling. In this manuscript, we present evidence to support the identification of the Eyes Absent (EYA) phosphatases, protein tyrosine phosphatases of the haloacid dehalogenase superfamily, as being capable of dephosphorylating the C-terminal tyrosyl residue of histone H2A.X. We demonstrate that EYA2 and EYA3 displayed specificity for Tyr-142 of H2A.X in assays in vitro. Suppression of eya3 by RNA interference resulted in elevated basal phosphorylation, and inhibited DNA damage-induced dephosphorylation, of Tyr-142 of H2A.X in vivo. The study provides the first indication of a physiological substrate for the EYA phosphatases and suggests a novel role for these enzymes in the regulation of the DNA damage response
Technology modules in the West Allis School District meeting Wisconsin state standards for technology education
No full textPlan BOver the years there has been a transition from vocational shop classes to what is now called technology education. Many schools are changing their classroom structure from a traditional style of teaching to modular instruction. With this evolution, various questions can be raised. There are many companies that manufacture technology modules, which modules will be chosen? Which modules best fit the curriculum? The biggest concern is whether the modules meet the current state standards. The Wisconsin State Standards have only been implemented since 1998. Technology modules are also a newer concept for technology education classrooms. The purpose of this study is to evaluate how well technology education modules meet the current Wisconsin Model Academic Standards for Technology Education, published by the Wisconsin Department of Public Instruction (1998). There are a variety of reasons this research was done. Technology modules have not been around long in classroom settings. Another reason would be the advent of new technology education standards brought forth by the state of Wisconsin. There has been an increase of school districts implementing modular classrooms. This study would be an asset to any district thinking about technology modules for their classes, and if they do meet state standards. This study may also help determine if technology modules purchased prior to 1998 meet current state standards. There are four main content standards within the Wisconsin Model Academic Standards for Technology Education: Human Ingenuity, Systems, The Nature of Technology, and The Impact of Technology. Each category contains specific performance standards that students will need to pass by the end of fourth, eighth, and twelfth grades. Scantech technology modules were used for this study because those are the modules used in the West Allis school district. The technology modules used are for the eighth grade “tech mods” class at the two middle schools. The module’s competencies were evaluated to see whether they met the Wisconsin standards for technology educatio
TALKING SCIENCE
No full textPresented as The Rockefeller University\u27s 54th Annual Alfred E. Mirsky Holiday Lecture on Science for high school students Epigenetics: Inheriting More than Genes delivered by C. David Allis, Ph.D.https://digitalcommons.rockefeller.edu/posters/1193/thumbnail.jp
The n-SET Domain of Set1 Regulates H2B Ubiquitylation-Dependent H3K4 Methylation
No full textPast studies have documented a crosstalk between H2B ubiquitylation (H2Bub) and H3K4 methylation, but little (if any) direct evidence exists explaining the mechanism underlying H2Bub-dependent H3K4 methylation on chromatin templates. Here, we took advantage of an in vitro histone methyltransferase assay employing a reconstituted yeast Set1 complex (ySet1C) and a recombinant chromatin template containing fully ubiquitylated H2B to gain valuable insights. Combined with genetic analyses, we demonstrate that the n-SET domain within Set1, but not Swd2, is essential for H2Bub-dependent H3K4 methylation. Spp1, a homolog of human CFP1, is conditionally involved in this crosstalk. Our findings extend to the human Set1 complex, underscoring the conserved nature of this disease-relevant crosstalk pathway. As not all members of the H3K4 methyltransferase family contain n-SET domains, our studies draw attention to the n-SET domain as a predictor of an H2B ubiquitylation-sensing mechanism that leads to downstream H3K4 methylation
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H3R42me2a is a histone modification with positive transcriptional effects
No full textProceedings of the National Academy of Sciences of the United States of America
Volume 110, Issue 37, 10 September 2013, Pages 14894-14899. Authors: Fabio Casadio, Xiangdong Lu, Samuel B. Pollock, Gary LeRoy, Benjamin A. Garcia, Thomas W. Muir (Tom W. Muir), Robert G. Roeder, and C. David Allis,Histone posttranslational modification leads to downstream effects indirectly by allowing or preventing docking of effector molecules, or directly by changing the intrinsic biophysical properties of local chromatin. To date, little has been done to study posttranslational modifications that lie outside of the unstructured tail domains of histones. Core residues, and in particular arginines in H3 and H4, mediate key interactions between the histone octamer and DNA in forming the nucleosomal particle. Using mass spectrometry, we find that one of these core residues, arginine 42 of histone H3 (H3R42), is dimethylated in mammalian cells by the methyltransferases coactivator arginine methyltransferase 1 (CARM1) and protein arginine methyltransferase 6 (PRMT6) in vitro and in vivo, and we demonstrate that methylation of H3R42 stimulates transcription in vitro from chromatinized templates. Thus, H3R42 is a new, "nontail" histone methylation site with positive effects on transcription. We propose that methylation of basic histone residues at the DNA interface may disrupt histone:DNA interactions, with effects on downstream processes, notably transcription
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