Abstract
Tremendous advances in the study of chromatin have revealed new classes of transcriptional regulators distinct from classical DNA-binding proteins. Many previously described transcription factors, coactivators, and adaptors are regulators of chromatin structure, interacting directly with the cove histone proteins or with nucleosomes. This review describes a method used by our laboratory to examine the interactions of regulatory proteins with the core histone proteins. Far-Western analysis uses a protein probe to detect interactions with histones immobilized on membranes. Variations of this technique can detect the acetylation state of the interacting histones and whether the interaction occurs through the globular domain or the amino-terminal 'tail' domain. In addition, we discuss complementary techniques for confirming histone-regulatory protein interactions.
Original language | English (US) |
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Pages (from-to) | 355-364 |
Number of pages | 10 |
Journal | Methods: A Companion to Methods in Enzymology |
Volume | 15 |
Issue number | 4 |
DOIs | |
State | Published - Aug 1998 |
ASJC Scopus subject areas
- Molecular Biology
- General Biochemistry, Genetics and Molecular Biology