Journal
METHODS
Volume 40, Issue 4, Pages 339-343Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymeth.2006.05.028
Keywords
histone modifications; peptide pull-down; chromatin; effector protein; historic methylation; histone acetylation; histone phosphorylation; biotinylated peptide
Funding
- NCRR NIH HHS [P41 RR001614] Funding Source: Medline
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Post-translational modifications of histories have been correlated with virtually all chromatin-templated processes, including gene expression regulation, DNA replication, mitosis and meiosis, and DNA repair. In order to better understand the mechanistic basis by which histone modifications participate in the control of cellular processes, it is essential to identify and characterize downstream effector proteins, or readers, that are responsible for recognizing different marks and translating them into specific biological outcomes. Ideally, identification of potential histone-binding effectors should occur in an unbiased fashion. Although in the recent years much progress has been made in identifying readers of histone modifications, in particular methylation, recognition of the majority of known histone marks is still poorly understood. Here I describe a simple and unbiased biochemical pull-down assay that allows for the identification of novel histone effector proteins and utilizes biotinylated histone peptides modified at various residues. I provide detailed protocols and suggestions for troubleshooting. (c) 2006 Elsevier Inc. All rights reserved.
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