Abstract
Histone proteins are the major protein components of chromatin - the physiologically relevant form of the genome (or epigenome) in all eukaryotic cells. For many years, histones were considered passive structural components of eukaryotic chromatin. In recent years, it has been demonstrated that dynamic association of histones and their variants to the genome plays a very important role in gene regulation. Histones are extensively modified during posttranslation viz. acetylation, methylation, phosphorylation, ubiquitylation, etc., and the identification of these covalent marks on canonical and variant histones is crucial for the understanding of their biological significance. Different biochemical techniques have been developed to purify and separate histone proteins; here, we describe techniques for analysis of histones from plant tissues.
Original language | English (US) |
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Pages (from-to) | 225-36 |
Number of pages | 12 |
Journal | Methods in molecular biology (Clifton, N.J.) |
Volume | 833 |
DOIs | |
State | Published - 2012 |
Keywords
- Acids
- Blotting, Western
- Chemical Fractionation
- Chromatography, High Pressure Liquid
- Chromatography, Reverse-Phase
- Electrophoresis, Polyacrylamide Gel
- Histones/isolation & purification
- Molecular Biology/methods
- Molecular Weight
- Mutant Proteins/isolation & purification
- Plant Proteins/isolation & purification
- Plants/metabolism
- Silver Staining
PubMed: MeSH publication types
- Journal Article
- Research Support, Non-U.S. Gov't