Biochemical analysis of chromatin structure and function using Drosophila embryo extracts

Methods : a Companion to Methods in Enzymology
T A BlankP B Becker

Abstract

The biochemical analysis of chromatin structure and function is greatly facilitated by the availability of cell-free systems that assemble chromatin under physiological conditions. One such system that has shown great potential is derived from extracts of early Drosophila embryos. These embryos contain large maternal stocks of chromatin constituents, such as histones and assembly factors. Chromatin assembled in these extracts resembles native chromatin in many respects: it displays physiological nucleosome repeat lengths, it is complex, containing a wealth of nonhistone proteins as well as enzymatic activities, and it has dynamic properties that allow the interaction of DNA-binding proteins that regulate important cellular processes. Most importantly, chromatin with variant properties, e.g., with respect to the basic geometry of the nucleosomal array, histone modifications, and its content of linker histones or nonhistone proteins, can be obtained by manipulating the reconstitution conditions. The synthesis of uniform chromatin with specific characteristics should allow the analysis of the functional significance of the structural and biochemical heterogeneity observed in vivo.

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Citations

Jan 10, 2003·Molecular Biology and Evolution·Vladimir V Kapitonov, Jerzy Jurka
Jun 17, 1998·Nucleic Acids Research·Z KaretsouT Papamarcaki
Nov 13, 2008·Molecular and Cellular Biology·Annette N D ScharfAxel Imhof
Mar 21, 1998·Proceedings of the National Academy of Sciences of the United States of America·W A Krajewski, P B Becker
May 23, 2015·Nucleic Acids Research·Alessandra GalatiStefano Cacchione
Jan 27, 2016·Molecular & Cellular Proteomics : MCP·Moritz Carl Völker-AlbertAxel Imhof
Nov 12, 2003·The EMBO Journal·Sven MoosmangNorbert Klugbauer
May 31, 2019·Nucleic Acids Research·Lisa HarpprechtPeter B Becker
Jul 27, 2001·The Journal of Biological Chemistry·S S NerA A Travers

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